Protein target profile

KP13_01964

Carbamoyl-phosphate synthase large chain

Genome: KpKP13 Gene: AHE46403.1 carB 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GME8

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Length 1074

Pocket druggability 0.918

Direct ligand evidence 0 102 total records

Functional annotation 2 EC 9 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: FPocket + P2Rank Both predictors report a high-scoring binding site (FPocket 0.92, P2Rank 0.91). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.92. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Review the complete evidence below

Risks to review

Evidence gaps

No metabolic context No SBML/network-derived reaction evidence is loaded for this protein.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 44.529 Lower values reduce human off-target concern.
Human E-value: 0.0
Gut microbiome similarity: 24.6% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 76.493 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Unknown

Structure confidence

ColabFold pLDDT: 96.45 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.918

Structure A0A0H3GME8

Pocket Pocket 1

P2Rank 0.911

Structure A0A0H3GME8

Pocket Pocket 1

ColabFold model

FPocket 0.698 · Pocket 64

P2Rank 0.886 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1165 / 4744 genomes with a hit

Prevalence 24.6%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GME8

Chemistry

ChEMBL CHEMBL4466052 ChEMBL CHEMBL4518489 ChEMBL CHEMBL4530311 ChEMBL CHEMBL4459017 ChEMBL CHEMBL4649653 ChEMBL CHEMBL4450292 ChEMBL CHEMBL4563086 ChEMBL CHEMBL4445287 ChEMBL CHEMBL4551132 ChEMBL CHEMBL4649844 ChEMBL CHEMBL4564355 ChEMBL CHEMBL4582507 ChEMBL CHEMBL4638888 ChEMBL CHEMBL57531 ChEMBL CHEMBL4440951 ChEMBL CHEMBL4464608 ChEMBL CHEMBL58627 ChEMBL 374 ChEMBL CHEMBL4634845 ChEMBL CHEMBL4644019 ChEMBL CHEMBL4520904 ChEMBL CHEMBL4634332 ChEMBL CHEMBL1201780

Sequence

Primary amino-acid sequence viewer.

MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGINGLDADFLRTLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECESNPSVDRDKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEQDLRRYFQTAVSVSNDAPVLLDRFLDDAIEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSKEIQDVMREQVQKLAFELQVRGLMNVQFAVKDNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGVTKEIIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKQGRALLSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTAGRQAIEDSKLIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQITK

MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVRKIIEKERPDAVLPTMGGQTALNCALELERQGVLAEFGVTMIGATADAIDKAEDRRRFDIAMKKIGLDTARSGIAHTMEEALAVAADVGFPCIIRPSFTMGGTGGGIAYNREEFEEICERGLDLSPTNELLIDESLIGWKEYEMEVVRDKNDNCIIVCSIENFDAMGIHTGDSITVAPAQTLTDKEYQIMRNASMAVLREIGVETGGSNVQFAVNPKNGRLIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELMNDITGGRTPASFEPSIDYVVTKIPRFNFEKFAGANDRLTTQMKSVGEVMAIGRTQQESLQKALRGLEVGATGFDPKVSLDDPEALTKIRRELKDAGAERIWYIADAFRAGLSVDGVFNLTNIDRWFLVQIEELVRLEEKVAEVGINGLDADFLRTLKRKGFADARLAKLAGVREAEIRKLRDQYDLHPVYKRVDTCAAEFATDTAYMYSTYEEECESNPSVDRDKIMVLGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPVTLEDVLEIVRIEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSPDAIDRAEDRERFQHAVDRLKLKQPANATVTAIEQAVEKAKEIGYPLVVRPSYVLGGRAMEIVYDEQDLRRYFQTAVSVSNDAPVLLDRFLDDAIEVDVDAICDGEMVLIGGIMEHIEQAGVHSGDSACSLPAYTLSKEIQDVMREQVQKLAFELQVRGLMNVQFAVKDNEVYLIEVNPRAARTVPFVSKATGVPLAKVAARVMAGKTLAQQGVTKEIIPPYYSVKEVVLPFNKFPGVDPLLGPEMRSTGEVMGVGRTFAEAFAKAQLGSNSTMKKQGRALLSVREGDKERVVDLAAKLLKFGFELDATHGTAIVLGEAGINPRLVNKVHEGRPHIQDRIKNGEYTYIINTTAGRQAIEDSKLIRRSALQYKVHYDTTLNGGFATAMALNADATEKVISVQEMHAQITK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 9 GO

Enzyme Commission (EC)

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
GO:0046872 Binding to a metal ion.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0004087 Catalysis of the reaction: 2 ATP + hydrogencarbonate + NH4+ = 2 ADP + carbamoyl phosphate + 2 H+ + phosphate.
GO:0004088 Catalysis of the reaction: hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H+.
GO:0044205 The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD+ or oxygen.
GO:0006541 The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
GO:0006526 The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

80 records

Show feature table

Start	End	DB	Term	Name
119	403	FunFam	G3DSA:3.30.470.20:FF:000007	Carbamoyl-phosphate synthase large chain
427	505	Pfam	PF02787	Carbamoyl-phosphate synthetase large chain, oligomerisation domain
427	505	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
554	663	FunFam	G3DSA:3.40.50.20:FF:000003	Carbamoyl-phosphate synthase large chain
1	8	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
1	116	Gene3D	G3DSA:3.40.50.20	-
396	554	SUPERFAMILY	SSF48108	Carbamoyl phosphate synthetase, large subunit connection domain
396	554	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
1	127	SUPERFAMILY	SSF52440	PreATP-grasp domain
1	127	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
6	1067	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
404	553	Gene3D	G3DSA:1.10.1030.10	-
404	553	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
119	403	Gene3D	G3DSA:3.30.470.20	-
405	553	FunFam	G3DSA:1.10.1030.10:FF:000002	Carbamoyl-phosphate synthase large chain
839	846	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
839	846	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
937	1074	ProSiteProfiles	PS51855	MGS-like domain profile.
937	1074	InterPro	IPR011607	Methylglyoxal synthase-like domain
666	936	FunFam	G3DSA:3.30.470.20:FF:000013	Carbamoyl-phosphate synthase large chain
674	934	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
957	1041	Pfam	PF02142	MGS-like domain
957	1041	InterPro	IPR011607	Methylglyoxal synthase-like domain
666	936	Gene3D	G3DSA:3.30.470.20	-
1	116	FunFam	G3DSA:3.40.50.20:FF:000001	Carbamoyl-phosphate synthase large chain
710	724	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
710	724	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
17	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
687	756	FunFam	G3DSA:3.30.1490.20:FF:000001	Carbamoyl-phosphate synthase large chain
297	304	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
297	304	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
554	663	Gene3D	G3DSA:3.40.50.20	-
5	1068	Hamap	MF_01210_A	Carbamoyl-phosphate synthase large chain [carB].
5	1068	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
133	328	ProSiteProfiles	PS50975	ATP-grasp fold profile.
133	328	InterPro	IPR011761	ATP-grasp fold
557	676	SUPERFAMILY	SSF52440	PreATP-grasp domain
557	676	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
164	178	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
164	178	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
2	1053	NCBIfam	TIGR01369	carbamoyl-phosphate synthase (glutamine-hydrolyzing) large subunit
2	1053	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
128	401	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region
1	1063	Hamap	MF_01210_B	Carbamoyl-phosphate synthase large chain [carB].
1	1063	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
424	547	SMART	SM01096	CPSase_L_D3_2
424	547	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
679	870	ProSiteProfiles	PS50975	ATP-grasp fold profile.
679	870	InterPro	IPR011761	ATP-grasp fold
943	1052	CDD	cd01424	MGS_CPS_II
943	1052	InterPro	IPR033937	Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain
9	16	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
937	1073	Gene3D	G3DSA:3.40.50.1380	-
937	1073	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
674	876	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
674	876	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
128	334	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
128	334	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
956	1042	SMART	SM00851	MGS_2a
956	1042	InterPro	IPR011607	Methylglyoxal synthase-like domain
380	398	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
380	398	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
19	33	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
19	33	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
48	58	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
48	58	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
204	223	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
204	223	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
239	256	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
239	256	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
297	326	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
297	326	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
168	180	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
168	180	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
938	1071	SUPERFAMILY	SSF52335	Methylglyoxal synthase-like
938	1071	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
22	1074	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1	24	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
937	1073	FunFam	G3DSA:3.40.50.1380:FF:000004	Carbamoyl-phosphate synthase large chain

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.918

Likely same site as P2Rank 3 1.3 Å 26 shared residues 100% of smaller site

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Surrounding area

Site 2 FPocket #45

0.57

Unusual size

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.911

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Surrounding area

Site 2 P2Rank #2

0.839

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Surrounding area

Site 3 P2Rank #3

0.811

Likely same site as FPocket 1 1.3 Å 26 shared residues 100% of smaller site

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Surrounding area

Site 4 P2Rank #4

0.744

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Surrounding area

Site 5 P2Rank #5

0.552

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Surrounding area

Residue sets

UniProt: Binding site:129-129

UniProt: Binding site:169-169

UniProt: Binding site:175-175

UniProt: Binding site:176-176

UniProt: Binding site:208-208

UniProt: Binding site:210-210

UniProt: Binding site:215-215

UniProt: Binding site:241-241

UniProt: Binding site:242-242

UniProt: Binding site:243-243

UniProt: Binding site:285-285

UniProt: Binding site:299-299

UniProt: Binding site:301-301

UniProt: Binding site:715-715

UniProt: Binding site:754-754

UniProt: Binding site:756-756

UniProt: Binding site:761-761

UniProt: Binding site:786-786

UniProt: Binding site:787-787

UniProt: Binding site:788-788

UniProt: Binding site:789-789

UniProt: Binding site:829-829

UniProt: Binding site:841-841

UniProt: Binding site:843-843

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #64

0.698

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Surrounding area

Site 2 FPocket #1

0.591

Likely same site as P2Rank 2 1.3 Å 31 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #6

0.478

Likely same site as P2Rank 1 0.9 Å 21 shared residues 100% of smaller site

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Surrounding area

Site 4 FPocket #65

0.222

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.886

Likely same site as FPocket 6 0.9 Å 21 shared residues 100% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.882

Likely same site as FPocket 1 1.3 Å 31 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.865

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Surrounding area

Site 4 P2Rank #4

0.684

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Surrounding area

Site 5 P2Rank #5

0.481

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A0H3GME8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_01964	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

102 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 52 records from similar proteins

Structural ligands 29 0 loaded crystals

Measured bioactivity 23 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0L1 PDB via homolog 146.1 Da · LogP 0.72 · TPSA 74.6 Open detail RCSB PDB

3NP PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

CAC PDB via homolog Detail RCSB PDB

F9V PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
0L1 RCSB PDB	4UTZ	P31327	146.1 Da LogP 0.72 TPSA 74.6	✓ Ro5	✓ Clean	`C(CCC(=O)O)CC(=O)O`
3NP RCSB PDB	4UTX	P31327	119.1 Da LogP -0.26 TPSA 80.4	✓ Ro5	✓ Clean	`C(C[N+](=O)[O-])C(=O)O`
ANP RCSB PDB	1BXR	P00968	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
CAC RCSB PDB	3OUU	Q0P8W7	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
F9V RCSB PDB	4UTV	P31327	194.2 Da LogP 1.33 TPSA 74.6	✓ Ro5	✓ Clean	`c1ccc(cc1)C(CC(=O)O)C(=O)O`
GUA RCSB PDB	4UTR	P31327	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
IMP RCSB PDB	1CE8	P00968	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O…`
JO3 RCSB PDB	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`CC(CC(=O)O)C(=O)O`
JZK RCSB PDB	3JZF	P24182	396.9 Da LogP 4.98 TPSA 72.9	✓ Ro5	✓ Clean	`c1ccc(c(c1)CNc2nc3cc(ccc3n2CC4CCCCC4)C(=O)N)Cl`
JZL RCSB PDB	3JZI	P24182	442.0 Da LogP 3.92 TPSA 119.2	✓ Ro5	✓ Clean	`c1ccc(c(c1)CNc2nc3cc(cc(c3n2C[C@@H]4CCCCC[C@@H]…`
L21 RCSB PDB	2W6Z	P24182	203.2 Da LogP 1.33 TPSA 69.6	✓ Ro5	✓ Clean	`CC(=CCn1cnc(c-2ncnc12)N)C`
L22 RCSB PDB	2W70	P24182	193.2 Da LogP 0.76 TPSA 90.7	✓ Ro5	✓ Clean	`c1cnc(nc1c2csc(n2)N)N`
L23 RCSB PDB	2W71	P24182	334.2 Da LogP 3.59 TPSA 69.6	✓ Ro5	✓ Clean	`Cc1nc(cn1Cc2c(cccc2Cl)Cl)c3ccnc(n3)N`
MLT RCSB PDB	3OUZ	Q0P8W7	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
MQM RCSB PDB	6OI9	P24182	389.3 Da LogP 3.37 TPSA 94.0	✓ Ro5	✓ Clean	`c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4CC[C@H](C4)CN)N…`
NLG RCSB PDB	5DOU	P31327	189.2 Da LogP -0.56 TPSA 103.7	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CCC(=O)O)C(=O)O`
NX6 RCSB PDB	4UUA	P31327	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`c1ccc(cc1)COC(=O)N[C@@H](CC(=O)O)C(=O)O`
OA1 RCSB PDB	2W6M	P24182	267.1 Da LogP 2.25 TPSA 69.1	✓ Ro5	✓ Clean	`c1cc(cc(c1)Br)C(=O)c2cnc(o2)N`
OA2 RCSB PDB	2W6N	P24182	307.4 Da LogP 3.10 TPSA 72.4	✓ Ro5	✓ Clean	`c1ccc(cc1)CN(Cc2ccccc2)C(=O)c3cnc(o3)N`
OA3 RCSB PDB	2W6O	P24182	191.2 Da LogP 1.21 TPSA 68.9	✓ Ro5	✓ Clean	`CC1(Cc2c(c(ncn2)N)C(=O)C1)C`
OA4 RCSB PDB	2W6P	P24182	250.3 Da LogP 2.77 TPSA 77.8	✓ Ro5	✓ Clean	`Cc1c(ccc2c1c(nc(n2)N)N)c3ccccc3`
OA5 RCSB PDB	2W6Q	P24182	247.3 Da LogP 0.49 TPSA 109.2	✓ Ro5	✓ Clean	`c1ccc(cc1)OCCOc2nc(nc(n2)N)N`
ORN RCSB PDB	1CE8	P00968	132.2 Da LogP -0.86 TPSA 89.3	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CN`
Q5A RCSB PDB	6UEL	P31327	390.5 Da LogP 3.49 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(n1)NC(=O)C2CCN(CC2)C(=O)N(C)Cc3ccc(cc3)F`
SRT RCSB PDB	3OUZ	Q0P8W7	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@H]([C@H](C(=O)O)O)(C(=O)O)O`
SU8 RCSB PDB	4UUB	P31327	174.2 Da LogP 1.35 TPSA 74.6	✓ Ro5	✓ Clean	`CCCC[C@H](CC(=O)O)C(=O)O`
SUH RCSB PDB	4UU7	P31327	132.1 Da LogP 0.18 TPSA 74.6	✓ Ro5	✓ Clean	`C[C@@H](CC(=O)O)C(=O)O`
TLA RCSB PDB	3OUZ	Q0P8W7	150.1 Da LogP -2.12 TPSA 115.1	✓ Ro5	✓ Clean	`[C@@H]([C@H](C(=O)O)O)(C(=O)O)O`
WOC RCSB PDB	4UU8	P31327	146.1 Da LogP 0.57 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)(CC(=O)O)C(=O)O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL4466052 ChEMBL	P37798	7.50 ~31.6 nM	378.8 Da LogP 3.58 TPSA 112.8	✓ Ro5	✓ Clean	`COc1ccc(-c2cccc(Cl)c2-c2cc3cnc(N)nc3nc2N)cn1`
CHEMBL4518489 ChEMBL	P37798	7.48 ~33.1 nM	387.3 Da LogP 2.97 TPSA 94.0	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3C[C@@H]4[C@@H](N)…`
CHEMBL4530311 ChEMBL	P37798	7.44 ~36.3 nM	348.8 Da LogP 3.57 TPSA 103.6	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3-c3cccnc3)c(N)nc2n1`
CHEMBL4459017 ChEMBL	P37798	7.19 ~64.6 nM	389.3 Da LogP 3.37 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4649653 ChEMBL	P31327	7.18 ~66.1 nM	409.5 Da LogP 3.69 TPSA 65.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc4cc[nH]c4c3…`
CHEMBL4450292 ChEMBL	P37798	7.10 ~79.4 nM	313.4 Da LogP 3.52 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3ccccc3-c3ccccc3)c(N)nc2n1`
CHEMBL4563086 ChEMBL	P37798	7.08 ~83.2 nM	405.3 Da LogP 2.48 TPSA 114.2	✓ Ro5	✓ Clean	`NCC1(O)CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4445287 ChEMBL	P37798	7.03 ~93.3 nM	343.8 Da LogP 3.54 TPSA 99.9	✓ Ro5	✓ Clean	`CC(C)COc1cccc(Cl)c1-c1cc2cnc(N)nc2nc1N`
CHEMBL4551132 ChEMBL	P37798	6.89 ~128.8 nM	314.4 Da LogP 2.92 TPSA 103.6	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3ccccc3-c3cccnc3)c(N)nc2n1`
CHEMBL4649844 ChEMBL	P31327	6.89 ~128.8 nM	432.5 Da LogP 3.75 TPSA 59.1	✓ Ro5	✓ Clean	`CCOc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(OC)cc3F)…`
CHEMBL4564355 ChEMBL	P37798	6.85 ~141.3 nM	390.3 Da LogP 3.40 TPSA 88.2	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3CCC(CO)C3)nc2n1`
CHEMBL4582507 ChEMBL	P37798	6.77 ~169.8 nM	403.3 Da LogP 2.89 TPSA 111.0	✓ Ro5	✓ Clean	`NC(=O)C1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4638888 ChEMBL	P31327	6.77 ~169.8 nM	423.5 Da LogP 4.00 TPSA 65.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc4cc(C)[nH]c…`
CHEMBL57531 ChEMBL	P37798	6.75 ~177.8 nM	395.1 Da LogP 3.38 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Br)cccc3Br)c(N)nc2n1`
CHEMBL4440951 ChEMBL	P37798	6.72 ~190.5 nM	405.3 Da LogP 2.48 TPSA 114.2	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N3CCC(N)(CO)C3)nc2n1`
CHEMBL4464608 ChEMBL	P37798	6.50 ~316.2 nM	403.3 Da LogP 3.76 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)CC1`
CHEMBL58627 ChEMBL	P37798	6.50 ~316.2 nM	306.2 Da LogP 3.16 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Cl)cccc3Cl)c(N)nc2n1`
374 ChEMBL	P31327	6.44 ~363.1 nM	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`C[C@@H]1CN(C[C@H](N1C(=O)c2ccc(cc2F)OC)C)C(=O)c…`
CHEMBL4634845 ChEMBL	P31327	6.44 ~363.1 nM	402.4 Da LogP 3.66 TPSA 49.9	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(C)cc3F)[C…`
CHEMBL4644019 ChEMBL	P31327	6.42 ~380.2 nM	432.5 Da LogP 3.75 TPSA 59.1	✓ Ro5	✓ Clean	`CCOc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc(OC)cc3F)C…`
CHEMBL4520904 ChEMBL	P37798	6.36 ~436.5 nM	407.3 Da LogP 3.46 TPSA 94.0	✓ Ro5	✓ Clean	`NCC1(F)CCN(c2nc3nc(N)ncc3cc2-c2c(Cl)cccc2Cl)C1`
CHEMBL4634332 ChEMBL	P31327	6.27 ~537.0 nM	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2[C@H](C)CN(C(=O)c3ccc(OC)c(F)c3)…`
CHEMBL1201780 ChEMBL	P31327	—	190.2 Da LogP -1.03 TPSA 129.7	✓ Ro5	✓ Clean	`NC(=O)N[C@@H](CCC(=O)O)C(=O)O`

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC13862907 ZINC	1.000	395.1 Da LogP 3.38 TPSA 90.7	✓ Ro5	✓ Clean	`Nc1ncc2cc(-c3c(Br)cccc3Br)c(N)nc2n1`
ZINC14951284 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1532551 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC16969369 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@…`
ZINC1700285 ZINC	1.000	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC2004353 ZINC	1.000	267.2 Da LogP 0.84 TPSA 112.9	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC2209 ZINC	1.000	203.2 Da LogP 1.33 TPSA 69.6	✓ Ro5	✓ Clean	`CC(C)=CCn1cnc(N)c2ncnc1-2`
ZINC2382313256 ZINC	1.000	390.5 Da LogP 3.49 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(NC(=O)C2CCN(C(=O)N(C)Cc3ccc(F)cc3)CC2)n1`
ZINC2557486 ZINC	1.000	334.2 Da LogP 3.59 TPSA 69.6	✓ Ro5	✓ Clean	`Cc1nc(-c2ccnc(N)n2)cn1Cc1c(Cl)cccc1Cl`
ZINC4228242 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@…`
ZINC4353761 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC8614392 ZINC	1.000	348.2 Da LogP -2.15 TPSA 180.0	✓ Ro5	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C…`
ZINC1529497 ZINC	0.917	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.917	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115 ZINC	0.917	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.917	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.917	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.917	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.917	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC1689810 ZINC	0.853	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC1708468 ZINC	0.853	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(C[C@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`
ZINC1845191 ZINC	0.853	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(C[C@@H](NC(=O)OCc1ccccc1)C(=O)O)OCc1ccccc1`
ZINC2022596 ZINC	0.853	266.3 Da LogP 0.24 TPSA 118.7	✓ Ro5	✓ Clean	`NC(=O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC106686432 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP…`
ZINC12958393 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)O…`
ZINC35024781 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024785 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC35024786 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)…`
ZINC4261903 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC80601236 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)O…`
ZINC95921560 ZINC	0.849	428.2 Da LogP -2.03 TPSA 226.5	2 viol.	✓ Clean	`O=c1[nH]cnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)O…`
ZINC170610434 ZINC	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@H](C)N(C(=O)c3ccc(OC)cc3F)[C…`
ZINC170610435 ZINC	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@H](C)N(C(=O)c3ccc(OC)cc3F)[C…`
ZINC170610436 ZINC	0.844	418.4 Da LogP 3.36 TPSA 59.1	✓ Ro5	✓ Clean	`COc1ccc(C(=O)N2C[C@@H](C)N(C(=O)c3ccc(OC)cc3F)[…`
ZINC1702215 ZINC	0.824	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)C[C@H](NC(=O)OCc1ccccc1)C(=O)OCc1ccccc1`
ZINC1744563 ZINC	0.824	357.4 Da LogP 2.50 TPSA 101.9	✓ Ro5	✓ Clean	`O=C(O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)OCc1ccccc1`
ZINC66267769 ZINC	0.821	372.5 Da LogP 3.35 TPSA 65.5	✓ Ro5	✓ Clean	`Cc1csc(NC(=O)C2CCN(C(=O)N(C)Cc3ccccc3)CC2)n1`
ZINC12360002 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@](=O)(O)OP(=O)(…`
ZINC31977053 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.810	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC107269764 ZINC	0.806	265.3 Da LogP 1.35 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)C[C@H](NC(=O)OCc1ccccc1)C(=O)O`
ZINC107269767 ZINC	0.806	265.3 Da LogP 1.35 TPSA 92.7	✓ Ro5	✓ Clean	`CC(=O)C[C@@H](NC(=O)OCc1ccccc1)C(=O)O`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.