Protein target profile

VK055_4666

guaA GMP synthetase

Genome: KpATCC43816 Gene: AIK83200.1 guaA 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GRL9

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Length 525

Pocket druggability 0.019

Metabolic reactions 3

Chokepoint No

Direct ligand evidence 0 53 total records

Functional annotation 0 EC 5 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

Central metabolic position More central than 91.4% of genes in this genome. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.92. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Human similarity Top human hit identity: 36.477%. Microbiome similarity 2241 of 4744 screened genomes (47.2%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.02.

Evidence coverage

Core evidence streams are available for this target.

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 (%): 36.477 Lower values reduce human off-target concern.
Human E-value: 2.23e-93
Gut microbiome similarity: 47.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 96.19 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 91.84 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 0.019

Structure A0A0H3GRL9

Pocket Pocket 25

P2Rank 0.918

Structure A0A0H3GRL9

Pocket Pocket 1

ColabFold model

FPocket 0.518 · Pocket 2

P2Rank 0.904 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 2241 / 4744 genomes with a hit

Prevalence 47.2%

Cross-references

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

Sequence

UniProt A0A0H3GRL9

Pathways

KEGG R01230 BioCyc GMP-SYN-NH3-RXN KEGG R00256 BioCyc GLUTAMIN-RXN KEGG R01231 BioCyc GMP-SYN-GLUT-RXN

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Metabolic context: more central than 91.4% of genes in this genome.

Relative network centrality 91.4% more central than 91.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIREFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEGSNEREFGYAQVEVVNDSALVRGIEDSLTADGKPLLDVWMSHGDKVTAIPADFVTVASTDNCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVERIRQQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAQQVMEMFGDHFGLNIVHVEGEQRFLDALAGESDPEAKRKIIGRVFVEVFDEEALKLDDVKWLAQGTIYPDVIESAASATGKAHVIKSHHNVGGLPKEMKMGLVEPLRELFKDEVRKIGLELGLPYDMLYRHPFPGPGLGVRVLGEVKKEYCDLLRRADAIFIEELHKADLYNKVSQAFTVFLPVRSVGVMGDGRKYDWVVSLRAVETIDFMTAHWAHLPYDFLGRVSNRIINEVNGISRVVYDISGKPPATIEWE

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0003921 Catalysis of the reaction: ATP + XMP + NH4+ = AMP + diphosphate + GMP + 2H+.
GO:0006177 The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate.
GO:0006164 The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
GO:0003922 Catalysis of the reaction: ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate + 2H+.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

41 records

Show feature table

Start	End	DB	Term	Name
9	207	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
12	199	Pfam	PF00117	Glutamine amidotransferase class-I
12	199	InterPro	IPR017926	Glutamine amidotransferase
209	410	FunFam	G3DSA:3.40.50.620:FF:000001	GMP synthase [glutamine-hydrolyzing]
209	410	Gene3D	G3DSA:3.40.50.620	HUPs
209	410	InterPro	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
411	525	FunFam	G3DSA:3.30.300.10:FF:000002	GMP synthase [glutamine-hydrolyzing]
212	525	NCBIfam	TIGR00884	glutamine-hydrolyzing GMP synthase, C-terminal domain
212	525	InterPro	IPR001674	GMP synthase, C-terminal
10	525	PANTHER	PTHR11922	GMP SYNTHASE-RELATED
177	190	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
54	63	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
81	92	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
217	258	Pfam	PF02540	NAD synthase
217	258	InterPro	IPR022310	NAD/GMP synthase
197	420	SUPERFAMILY	SSF52402	Adenine nucleotide alpha hydrolases-like
5	204	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
5	204	InterPro	IPR029062	Class I glutamine amidotransferase-like
405	525	SUPERFAMILY	SSF54810	GMP synthetase C-terminal dimerisation domain
433	524	Pfam	PF00958	GMP synthase C terminal domain
433	524	InterPro	IPR001674	GMP synthase, C-terminal
9	206	Gene3D	G3DSA:3.40.50.880	-
9	206	InterPro	IPR029062	Class I glutamine amidotransferase-like
411	525	Gene3D	G3DSA:3.30.300.10	-
7	206	FunFam	G3DSA:3.40.50.880:FF:000001	GMP synthase [glutamine-hydrolyzing]
10	198	CDD	cd01742	GATase1_GMP_Synthase
10	198	InterPro	IPR004739	GMP synthase, glutamine amidotransferase
7	525	Hamap	MF_00344	GMP synthase [glutamine-hydrolyzing] [guaA].
7	525	InterPro	IPR022955	GMP synthase
51	65	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
10	24	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
81	97	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
10	205	NCBIfam	TIGR00888	glutamine-hydrolyzing GMP synthase, N-terminal domain
10	205	InterPro	IPR004739	GMP synthase, glutamine amidotransferase
229	524	CDD	cd01997	GMP_synthase_C
229	524	InterPro	IPR001674	GMP synthase, C-terminal
208	400	ProSiteProfiles	PS51553	GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain profile.
208	400	InterPro	IPR025777	GMP synthetase ATP pyrophosphatase domain
81	92	PRINTS	PR00097	Anthranilate synthase component II signature
54	63	PRINTS	PR00097	Anthranilate synthase component II signature
177	190	PRINTS	PR00097	Anthranilate synthase component II signature

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 · P2Rank

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

Site 1 P2Rank #1

0.918

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Surrounding area

Site 2 P2Rank #2

0.238

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Surrounding area

Site 3 P2Rank #3

0.157

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Surrounding area

Site 4 P2Rank #4

0.102

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Surrounding area

Site 5 P2Rank #5

0.067

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Surrounding area

Residue sets

UniProt: Active site:181-181

UniProt: Active site:183-183

UniProt: Active site:86-86 Nucleophile

UniProt: Binding site:235-241

Binding pockets · FPocket

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

Site 1 FPocket #2

0.518

Likely same site as P2Rank 1 4.9 Å 16 shared residues 89% of smaller site

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Surrounding area

Site 2 FPocket #6

0.386

Likely same site as P2Rank 1 5.9 Å 19 shared residues 68% of smaller site

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

0.904

Likely same site as FPocket 2 4.9 Å 16 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.294

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Surrounding area

Site 3 P2Rank #3

0.119

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Surrounding area

Site 4 P2Rank #4

0.091

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Surrounding area

Site 5 P2Rank #5

0.089

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Surrounding area

Residue sets

UniProt: Active site:181-181

UniProt: Active site:183-183

UniProt: Active site:86-86 Nucleophile

UniProt: Binding site:235-241

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_A0A0H3GRL9	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4666	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.

53 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 3 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

MLA PDB via homolog 104.1 Da · LogP -0.45 · TPSA 74.6 Open detail RCSB PDB

POP PDB via homolog Detail RCSB PDB

XMP PDB via homolog Detail RCSB PDB

ZINC1532902 ZINC proposed compound · Tanimoto 0.700 Detail ZINC

ZINC2018106 ZINC proposed compound · Tanimoto 0.700 Detail ZINC

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
MLA RCSB PDB	6JP9	Q58531	104.1 Da LogP -0.45 TPSA 74.6	✓ Ro5	✓ Clean	`C(C(=O)O)C(=O)O`
POP RCSB PDB	1GPM	P04079	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
XMP RCSB PDB	2VXO	P49915	365.2 Da LogP -3.44 TPSA 201.2	1 viol.	✓ Clean	`c1[nH+]c2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=…`

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).

No ChEMBL hits found through similar proteins.

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
ZINC1532902 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@@](O)(CC(=O)O)C(=O)O`
ZINC2018106 ZINC	0.700	206.2 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC[C@](O)(CC(=O)O)C(=O)O`
ZINC1532710 ZINC	0.661	364.2 Da LogP -2.86 TPSA 200.0	1 viol.	✓ Clean	`O=c1[nH]c(=O)c2ncn([C@H]3O[C@@H](COP(=O)(O)O)[C…`
ZINC4228292 ZINC	0.661	364.2 Da LogP -2.86 TPSA 200.0	1 viol.	✓ Clean	`O=c1[nH]c(=O)c2ncn([C@@H]3O[C@H](COP(=O)(O)O)[C…`
ZINC2390999 ZINC	0.655	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](NC(=O)CC[C@H](N)C(=O)O)C(=O)O`
ZINC3593496 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC3593497 ZINC	0.652	206.2 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC14686440 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=O…`
ZINC14686442 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@](O)(CC(=O…`
ZINC14686444 ZINC	0.625	436.4 Da LogP -2.64 TPSA 247.9	1 viol.	✓ Clean	`O=C(O)C[C@@](O)(CC(=O)NCCCCNC(=O)C[C@@](O)(CC(=…`
ZINC3055005 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@H](N)C(=O)O)C(=O)O`
ZINC3055007 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC3055010 ZINC	0.591	204.2 Da LogP -0.63 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC2391099 ZINC	0.586	274.3 Da LogP -2.59 TPSA 178.6	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)O`
ZINC13398039 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@](O)(CC(=O)O)C(=O)O`
ZINC2528012 ZINC	0.577	234.2 Da LogP -0.38 TPSA 121.1	✓ Ro5	✓ Clean	`CC(C)OC(=O)C[C@@](O)(CC(=O)O)C(=O)O`
ZINC2556600 ZINC	0.567	217.2 Da LogP -1.83 TPSA 135.5	✓ Ro5	✓ Clean	`C[C@H](NC(=O)[C@@H](N)CCC(N)=O)C(=O)O`
ZINC1555366 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1555367 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1555369 ZINC	0.565	232.3 Da LogP 0.15 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720127 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@H](N)C(=O)O)C(=O)O`
ZINC1720128 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC1720130 ZINC	0.565	218.3 Da LogP -0.24 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](CCCCC[C@@H](N)C(=O)O)C(=O)O`
ZINC13515793 ZINC	0.561	338.2 Da LogP -2.43 TPSA 171.3	✓ Ro5	✓ Clean	`Cc1cn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H]2…`
ZINC13518175 ZINC	0.561	450.1 Da LogP -2.13 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC146315135 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@@](O)(CC(=O)O)C(=O)O`
ZINC146315336 ZINC	0.560	204.2 Da LogP 0.86 TPSA 94.8	✓ Ro5	✓ Clean	`CCCCC[C@](O)(CC(=O)O)C(=O)O`
ZINC1850353 ZINC	0.556	206.1 Da LogP -0.86 TPSA 132.1	✓ Ro5	✓ Clean	`O=C(O)CC(O)(CC(=O)O)CC(=O)O`
ZINC12503831 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]2…`
ZINC12503833 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H]…`
ZINC13512000 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC1532538 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC2026984 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H]…`
ZINC2123545 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC2606131 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC36377965 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@H](O)[C@@H…`
ZINC3870257 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC3870258 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC3870259 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@@…`
ZINC3870260 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@@H](O)[C@…`
ZINC9235501 ZINC	0.554	324.2 Da LogP -2.73 TPSA 171.3	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@@H](COP(=O)(O)O)[C@H](O)[C@H…`
ZINC1581634 ZINC	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)NCC(=O)O`
ZINC5500823 ZINC	0.552	203.2 Da LogP -2.22 TPSA 135.5	✓ Ro5	✓ Clean	`NC(=O)CC[C@@H](N)C(=O)NCC(=O)O`
ZINC13517211 ZINC	0.534	340.2 Da LogP -1.37 TPSA 154.2	✓ Ro5	✓ Clean	`O=c1ccn([C@@H]2O[C@H](COP(=O)(O)O)[C@@H](O)[C@H…`
ZINC9659886 ZINC	0.532	363.2 Da LogP -2.74 TPSA 206.8	1 viol.	✓ Clean	`N=c1[nH]c(=O)c2ncn([C@@H]3O[C@@H](COP(=O)(O)O)[…`
ZINC2560992 ZINC	0.531	275.3 Da LogP -1.99 TPSA 172.8	✓ Ro5	✓ Clean	`NC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(=O)O)C(=O)O`
ZINC205346095 ZINC	0.525	369.2 Da LogP -2.83 TPSA 214.4	✓ Ro5	✓ Clean	`O=c1[nH]c(=O)n([C@@H]2O[C@H](COP(=O)(O)O)[C@@H]…`
ZINC13398014 ZINC	0.522	220.2 Da LogP -1.07 TPSA 110.1	✓ Ro5	✓ Clean	`COC(=O)CC(O)(CC(=O)OC)C(=O)O`
ZINC3861629 ZINC	0.522	206.1 Da LogP -1.16 TPSA 121.1	✓ Ro5	✓ Clean	`COC(=O)C(O)(CC(=O)O)CC(=O)O`
ZINC2108714 ZINC	0.519	217.3 Da LogP 1.21 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CCCCCCCC(=O)O)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.