Protein target profile

HT085_RS00245

carbamoyl-phosphate synthase large subunit

Genome: NZ_AP023069.1 Gene: carB TUM19854C_00390 3D evidence: ColabFold model

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Length 1071

Direct ligand evidence 0 93 total records

Functional annotation 0 EC 2 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing 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
Gut microbiome off-target: Hit

Essentiality

Essential (DEG): Y

Localization

Localization: Unknown

Binding-site evidence

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 Low

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYKVILVNSNPATIMTDPEMADVTYIEPIMWQTVEKIIAKERPDAILPTMGGQTALNCALDLARNGVLAKYNVELIGATEDAIDKAEDRGRFKEAMEKIGLSCPKSFVCHTMNEALAAQEQVGFPTLIRPSFTMGGSGGGIAYNKDEFLAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNCIIICSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFAVNPENGEMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGFTLDELRNDITGGRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTIQESFQKALRGLETGLCGFNPRSEDKAEIRRELANPGPERMLFVADAFRAGFTPEEIHEICAIDPWFLAQIEDLMKEEKSVSDGQLQDLDYAALRRLKRKGFSDKRLAQLLNVSEKEVREHRYALKLHPVYKRADTCAAEFATETAYLYSTYEEECESRPSDRKKVMILGGGPNRIGQGIEFDYCCVHAALALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRTENPWGVIVHYGGQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLNDLGLRQPPNRIAHNEEEALVKAEEIGYPLVVRPSYVLGGRAMQIVHSAEALQKYMREAVQVSEDSPVLLDFFLNNAIEVDVDCVSDGKDVVIGGIMQHVEQAGIHSGDSGCSLPPYSLSEEIQDEIRRQTKAMAYALGVVGLMNVQFAVQDGVVFVLEVNPRASRTVPFVSKATGVPLAKVGARCMAGISLKEQGVEKEVVPDFYAVKEAVFPFIKFPGVDTILSPEMRSTGEVMGVGASFGEAYYKAQLGAGERLNPTGKIFLSVREEDKERVIKTAKNFQALGYGICATRGTAQYLTEHGLIVQAINKVPEGRPHIGDALKNGEIALVVNTVSSDPQSVSDSHIIRQSALQQRVPQYTTTAGGEAMSEGAKSRDYLGVYSVQELHGRLKNRN

MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYKVILVNSNPATIMTDPEMADVTYIEPIMWQTVEKIIAKERPDAILPTMGGQTALNCALDLARNGVLAKYNVELIGATEDAIDKAEDRGRFKEAMEKIGLSCPKSFVCHTMNEALAAQEQVGFPTLIRPSFTMGGSGGGIAYNKDEFLAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKADNCIIICSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFAVNPENGEMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGFTLDELRNDITGGRTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTIQESFQKALRGLETGLCGFNPRSEDKAEIRRELANPGPERMLFVADAFRAGFTPEEIHEICAIDPWFLAQIEDLMKEEKSVSDGQLQDLDYAALRRLKRKGFSDKRLAQLLNVSEKEVREHRYALKLHPVYKRADTCAAEFATETAYLYSTYEEECESRPSDRKKVMILGGGPNRIGQGIEFDYCCVHAALALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRTENPWGVIVHYGGQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLNDLGLRQPPNRIAHNEEEALVKAEEIGYPLVVRPSYVLGGRAMQIVHSAEALQKYMREAVQVSEDSPVLLDFFLNNAIEVDVDCVSDGKDVVIGGIMQHVEQAGIHSGDSGCSLPPYSLSEEIQDEIRRQTKAMAYALGVVGLMNVQFAVQDGVVFVLEVNPRASRTVPFVSKATGVPLAKVGARCMAGISLKEQGVEKEVVPDFYAVKEAVFPFIKFPGVDTILSPEMRSTGEVMGVGASFGEAYYKAQLGAGERLNPTGKIFLSVREEDKERVIKTAKNFQALGYGICATRGTAQYLTEHGLIVQAINKVPEGRPHIGDALKNGEIALVVNTVSSDPQSVSDSHIIRQSALQQRVPQYTTTAGGEAMSEGAKSRDYLGVYSVQELHGRLKNRN

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

73 records

Show feature table

Start	End	DB	Term	Name
931	1071	ProSiteProfiles	PS51855	MGS-like domain profile.
931	1071	InterPro	IPR011607	Methylglyoxal synthase-like domain
552	670	SUPERFAMILY	SSF52440	PreATP-grasp domain
552	670	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
1069	1071	Coils	Coil	Coil
419	542	SMART	SM01096	CPSase_L_D3_2
419	542	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
668	870	Pfam	PF02786	Carbamoyl-phosphate synthase L chain, ATP binding domain
668	870	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
168	180	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
168	180	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
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
204	223	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
204	223	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
297	326	PRINTS	PR00098	Carbamoyl-phosphate synthase protein CPSase domain signature
297	326	InterPro	IPR005483	Carbamoyl-phosphate synthase large subunit, CPSase domain
422	500	Pfam	PF02787	Carbamoyl-phosphate synthetase large chain, oligomerisation domain
422	500	InterPro	IPR005480	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain
396	549	SUPERFAMILY	SSF48108	Carbamoyl phosphate synthetase, large subunit connection domain
396	549	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
931	1066	SUPERFAMILY	SSF52335	Methylglyoxal synthase-like
931	1066	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
119	403	FunFam	G3DSA:3.30.470.20:FF:000007	Carbamoyl-phosphate synthase large chain
6	1051	PANTHER	PTHR11405	CARBAMOYLTRANSFERASE FAMILY MEMBER
1	116	Gene3D	G3DSA:3.40.50.20	-
660	930	FunFam	G3DSA:3.30.470.20:FF:000013	Carbamoyl-phosphate synthase large chain
2	1046	NCBIfam	TIGR01369	carbamoyl-phosphate synthase (glutamine-hydrolyzing) large subunit
2	1046	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
403	548	Gene3D	G3DSA:1.10.1030.10	-
403	548	InterPro	IPR036897	Carbamoyl-phosphate synthetase, large subunit oligomerisation domain superfamily
297	304	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
297	304	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
1	116	FunFam	G3DSA:3.40.50.20:FF:000001	Carbamoyl-phosphate synthase large chain
668	928	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
704	718	ProSitePatterns	PS00866	Carbamoyl-phosphate synthase subdomain signature 1.
704	718	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
133	328	ProSiteProfiles	PS50975	ATP-grasp fold profile.
133	328	InterPro	IPR011761	ATP-grasp fold
681	750	FunFam	G3DSA:3.30.1490.20:FF:000001	Carbamoyl-phosphate synthase large chain
950	1037	SMART	SM00851	MGS_2a
950	1037	InterPro	IPR011607	Methylglyoxal synthase-like domain
128	401	SUPERFAMILY	SSF56059	Glutathione synthetase ATP-binding domain-like
1	127	SUPERFAMILY	SSF52440	PreATP-grasp domain
1	127	InterPro	IPR016185	Pre-ATP-grasp domain superfamily
833	840	ProSitePatterns	PS00867	Carbamoyl-phosphate synthase subdomain signature 2.
833	840	InterPro	IPR005479	Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain
405	548	FunFam	G3DSA:1.10.1030.10:FF:000002	Carbamoyl-phosphate synthase large chain
549	657	FunFam	G3DSA:3.40.50.20:FF:000003	Carbamoyl-phosphate synthase large chain
119	402	Gene3D	G3DSA:3.30.470.20	-
937	1047	CDD	cd01424	MGS_CPS_II
937	1047	InterPro	IPR033937	Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain
549	657	Gene3D	G3DSA:3.40.50.20	-
951	1037	Pfam	PF02142	MGS-like domain
951	1037	InterPro	IPR011607	Methylglyoxal synthase-like domain
1	1058	Hamap	MF_01210_B	Carbamoyl-phosphate synthase large chain [carB].
1	1058	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
5	1063	Hamap	MF_01210_A	Carbamoyl-phosphate synthase large chain [carB].
5	1063	InterPro	IPR006275	Carbamoyl-phosphate synthase, large subunit
932	1068	Gene3D	G3DSA:3.40.50.1380	-
932	1068	InterPro	IPR036914	Methylglyoxal synthase-like domain superfamily
660	930	Gene3D	G3DSA:3.30.470.20	-
1	24	ProSiteProfiles	PS51257	Prokaryotic membrane lipoprotein lipid attachment site profile.
673	864	ProSiteProfiles	PS50975	ATP-grasp fold profile.
673	864	InterPro	IPR011761	ATP-grasp fold

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 #6

0.335

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Surrounding area

Site 2 FPocket #4

0.306

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Surrounding area

All structural evidence 0 experimental · 1 predicted

Structural evidence

0 + 1

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
ColabFold HT085_RS00245	ColabFold	—	—	full sequence	—	Viewing

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.

93 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 43 records from similar proteins

Structural ligands 20 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

ACP PDB via homolog Detail RCSB PDB

ANP 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`
ACP RCSB PDB	4MV8	P43873	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
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)…`
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`
MQV RCSB PDB	6OI8	P43873	429.9 Da LogP 3.38 TPSA 106.8	✓ Ro5	✓ Clean	`c1cc(c(c(c1)Cl)c2cc3cnc(nc3nc2N4C[C@@H]5[C@H](C…`
MV4 RCSB PDB	6OJH	P43873	356.4 Da LogP 2.96 TPSA 94.0	✓ Ro5	✓ Clean	`c1ccc2c(c1)cccc2c3cc4cnc(nc4nc3N5CC[C@H](C5)N)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`
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`
PCT RCSB PDB	4MV6	P43873	139.0 Da LogP -1.35 TPSA 100.6	✓ Ro5	✓ Clean	`C(C(=O)N)P(=O)(O)O`
PPF RCSB PDB	4MV7	P43873	126.0 Da LogP -0.16 TPSA 94.8	✓ Ro5	✓ Clean	`C(=O)(O)P(=O)(O)O`
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`
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`
WOC RCSB PDB	4UU8	P31327	146.1 Da LogP 0.57 TPSA 74.6	✓ Ro5	✓ Clean	`CC(C)(CC(=O)O)C(=O)O`
Y7Y RCSB PDB	4RZQ	P43873	316.4 Da LogP 1.36 TPSA 84.9	✓ Ro5	✓ Clean	`COC(=O)CCCC[C@H]1[C@@H]2[C@H](CS1)N(C(=O)N2)C(=…`

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
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…`
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`
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`
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`
ZINC105469665 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=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`
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)[…`
ZINC103601590 ZINC	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC103601597 ZINC	0.840	286.4 Da LogP 4.47 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC1603111 ZINC	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC2027042 ZINC	0.840	258.4 Da LogP 3.69 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC2566748 ZINC	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@@H](CC(=O)O)C(=O)O`
ZINC3199210 ZINC	0.840	202.2 Da LogP 2.13 TPSA 74.6	✓ Ro5	✓ Clean	`CCCCCC[C@H](CC(=O)O)C(=O)O`
ZINC12360002 ZINC	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	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	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
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`
ZINC1532510 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=…`
ZINC1532511 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O…`
ZINC1532512 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O…`
ZINC1532513 ZINC	0.821	304.3 Da LogP -1.60 TPSA 170.1	✓ Ro5	✓ Clean	`CC(=O)N[C@H](CC(=O)O)C(=O)N[C@H](CCC(=O)O)C(=O)O`
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`
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.