KpATCC43816 Protein target profile

anthranilate synthase component II

Accession: VK055_1194

Gene: trpD AIK79817.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 1 reaction UniProt A0A0H3GLX6

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Length 531

Pocket druggability (P2Rank · AlphaFold DB model) 0.97

Metabolic reactions 1

Chokepoint Yes

Direct ligand evidence 0 67 total records

Functional annotation 0 EC 3 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 94.3% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Review the complete evidence below

Risks to review

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: No hit
Gut microbiome similarity: 1.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 56.995 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.72 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.97

Structure A0A0H3GLX6

Pocket Pocket 1

Druggability (FPocket) 0.783

Structure A0A0H3GLX6

Pocket Pocket 23

ColabFold model

P2Rank 0.964 · Pocket 1

FPocket 0.567 · Pocket 6

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 67 / 4744 genomes with a hit

Prevalence 1.4%

Cross-references

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

Sequence

UniProt A0A0H3GLX6

Pathways

KEGG R01073 BioCyc PRTRANS-RXN

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction in Phenylalanine, tyrosine and tryptophan biosynthesis, no isoenzyme backup detected, more central than 94.3% of genes in this genome, no human homolog detected.

Relative network centrality 94.3% more central than 94.3% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MADILLLDNIDSFTYNLADQLRANGHNVVIYRNSVPAQALIERLGTMDNPVLMLSPGPGTPSEAGCMPELLTRMRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNIPAGLTINANFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWALQKLEHTNTLQPILEKLYQAETLSQQESHQLFSAVVRGEVKPEQLAAALVSMKVRGEQPQEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRAALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTVVAELHNGEIKSYQLTADDFGLTPYHQAQLAGGTPEENRDILTRLLQGKGEAAHEAAVAANVAMLMRLHGHEDLKANAQQVLDVLHSGAAYDRVTALAARG

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0004048 Catalysis of the reaction: N-(5-phospho-beta-D-ribosyl)anthranilate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate.
GO:0016757 Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
GO:0000162 The chemical reactions and pathways resulting in the formation of L-tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; L-tryptophan is synthesized from chorismate via anthranilate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

42 records

Show feature table

Start	End	DB	Term	Name
197	524	PANTHER	PTHR43285	ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE
197	524	InterPro	IPR005940	Anthranilate phosphoribosyl transferase
192	275	FunFam	G3DSA:1.20.970.10:FF:000003	Anthranilate phosphoribosyltransferase
204	528	NCBIfam	TIGR01245	anthranilate phosphoribosyltransferase
204	528	InterPro	IPR005940	Anthranilate phosphoribosyl transferase
273	521	Pfam	PF00591	Glycosyl transferase family, a/b domain
273	521	InterPro	IPR000312	Glycosyl transferase, family 3
52	61	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
166	179	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
79	90	PRINTS	PR00096	Glutamine amidotransferase superfamily signature
269	530	FunFam	G3DSA:3.40.1030.10:FF:000002	Anthranilate phosphoribosyltransferase
4	186	NCBIfam	TIGR00566	glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase
4	186	InterPro	IPR006221	Anthranilate synthase/para-aminobenzoate synthase like domain
192	275	Gene3D	G3DSA:1.20.970.10	Transferase, Pyrimidine Nucleoside Phosphorylase; Chain C
4	187	CDD	cd01743	GATase1_Anthranilate_Synthase
4	187	InterPro	IPR006221	Anthranilate synthase/para-aminobenzoate synthase like domain
79	95	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
49	63	PRINTS	PR00099	Carbamoyl-phosphate synthase protein GATase domain signature
3	196	ProSiteProfiles	PS51273	Glutamine amidotransferase type 1 domain profile.
202	262	Pfam	PF02885	Glycosyl transferase family, helical bundle domain
202	262	InterPro	IPR017459	Glycosyl transferase family 3, N-terminal domain
2	191	Gene3D	G3DSA:3.40.50.880	-
2	191	InterPro	IPR029062	Class I glutamine amidotransferase-like
6	186	Pfam	PF00117	Glutamine amidotransferase class-I
6	186	InterPro	IPR017926	Glutamine amidotransferase
2	191	FunFam	G3DSA:3.40.50.880:FF:000021	Anthranilate phosphoribosyltransferase
3	191	SUPERFAMILY	SSF52317	Class I glutamine amidotransferase-like
3	191	InterPro	IPR029062	Class I glutamine amidotransferase-like
269	527	SUPERFAMILY	SSF52418	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
269	527	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
276	530	Gene3D	G3DSA:3.40.1030.10	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain
276	530	InterPro	IPR035902	Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain superfamily
200	266	SUPERFAMILY	SSF47648	Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain
200	266	InterPro	IPR036320	Glycosyl transferase family 3, N-terminal domain superfamily
124	136	PRINTS	PR00097	Anthranilate synthase component II signature
4	18	PRINTS	PR00097	Anthranilate synthase component II signature
79	90	PRINTS	PR00097	Anthranilate synthase component II signature
104	112	PRINTS	PR00097	Anthranilate synthase component II signature
166	179	PRINTS	PR00097	Anthranilate synthase component II signature
52	61	PRINTS	PR00097	Anthranilate synthase component II signature
202	530	Hamap	MF_00211	Anthranilate phosphoribosyltransferase [trpD].
202	530	InterPro	IPR005940	Anthranilate phosphoribosyl transferase

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

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.97

Likely same site as FPocket 23 2.1 Å 39 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.183

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Surrounding area

Pocket 3 P2Rank #3

0.009

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Surrounding area

Pocket 4 P2Rank #4

0.006

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Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #23

0.783 Unusual size

Likely same site as P2Rank 1 2.1 Å 39 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:278-278

UniProt: Binding site:281-282

UniProt: Binding site:286-286

UniProt: Binding site:288-291

UniProt: Binding site:290-290

UniProt: Binding site:306-314

UniProt: Binding site:309-309

UniProt: Binding site:318-318

UniProt: Binding site:364-364

UniProt: Binding site:422-422

UniProt: Binding site:423-423

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.964

Likely same site as FPocket 6 3.2 Å 35 shared residues 97% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.23

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Surrounding area

Pocket 3 P2Rank #3

0.225

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Surrounding area

Pocket 4 P2Rank #4

0.068

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Surrounding area

Residue sets

UniProt: Binding site:278-278

UniProt: Binding site:281-282

UniProt: Binding site:286-286

UniProt: Binding site:288-291

UniProt: Binding site:290-290

UniProt: Binding site:306-314

UniProt: Binding site:309-309

UniProt: Binding site:318-318

UniProt: Binding site:364-364

UniProt: Binding site:422-422

UniProt: Binding site:423-423

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_A0A0H3GLX6	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1194	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.

67 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 17 records from similar proteins

Structural ligands 17 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

17C PDB via homolog 257.2 Da · LogP 2.83 · TPSA 86.6 Open detail RCSB PDB

4M0 PDB via homolog Detail RCSB PDB

59L PDB via homolog Detail RCSB PDB

61L PDB via homolog Detail RCSB PDB

62L 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
17C RCSB PDB	4IJ1	P9WFX5	257.2 Da LogP 2.83 TPSA 86.6	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)O)Nc2ccccc2C(=O)O`
4M0 RCSB PDB	4OWS	P9WFX5	151.2 Da LogP 1.28 TPSA 63.3	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)N)C(=O)O`
59L RCSB PDB	4ZOF	A5U4M0	316.3 Da LogP 3.04 TPSA 129.8	✓ Ro5	✓ Clean	`Cc1cccc(c1Nc2cc(ccc2C(=O)O)[N+](=O)[O-])C(=O)O`
61L RCSB PDB	4ZOJ	A5U4M0	287.4 Da LogP 4.47 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)Nc2c(cccc2SC)C)C(=O)O`
62L RCSB PDB	4ZOK	A5U4M0	319.4 Da LogP 3.15 TPSA 83.5	✓ Ro5	✓ Clean	`Cc1ccc(c(c1)Nc2c(cccc2S(=O)(=O)C)C)C(=O)O`
644 RCSB PDB	4M0R	P9WFX5	392.4 Da LogP 4.27 TPSA 136.0	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)O)Nc2cccc(c2C(=O)O)Nc3ccccc3C(=…`
7P1 RCSB PDB	5BO2	A5U4M0	395.3 Da LogP 2.77 TPSA 153.4	✓ Ro5	Alert	`c1ccc(c(c1)C(=O)O)Nc2ccc(cc2C(=O)O)OCCCP(=O)(O)O`
7P2 RCSB PDB	5BO3	A5U4M0	409.3 Da LogP 3.16 TPSA 153.4	✓ Ro5	Alert	`c1ccc(c(c1)C(=O)O)Nc2ccc(cc2C(=O)O)OCCCCP(=O)(O…`
7P3 RCSB PDB	5BNE	P9WFX5	423.4 Da LogP 3.55 TPSA 153.4	✓ Ro5	Alert	`c1ccc(c(c1)C(=O)O)Nc2ccc(cc2C(=O)O)OCCCCCP(=O)(…`
BE2 RCSB PDB	4OWV	P9WFX5	137.1 Da LogP 0.97 TPSA 63.3	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)O)N`
BEN RCSB PDB	2BPQ	P9WFX5	120.2 Da LogP 0.97 TPSA 49.9	✓ Ro5	✓ Clean	`[H]/N=C(\c1ccccc1)/N`
CXS RCSB PDB	4HKM	Q8PD71	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`C1CCC(CC1)NCCCS(=O)(=O)O`
FA0 RCSB PDB	4N8Q	P9WFX5	155.1 Da LogP 1.11 TPSA 63.3	✓ Ro5	✓ Clean	`c1cc(c(cc1F)N)C(=O)O`
MLT RCSB PDB	4X58	P9WFX5	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@H](C(=O)O)O)C(=O)O`
POP RCSB PDB	4OWS	P9WFX5	176.0 Da LogP -2.08 TPSA 129.9	✓ Ro5	✓ Clean	`O[P@@](=O)([O-])O[P@@](=O)(O)[O-]`
PRP RCSB PDB	4ZOF	A5U4M0	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`C([C@@H]1[C@H]([C@H]([C@H](O1)O[P@@](=O)(O)OP(=…`
TA7 RCSB PDB	4ZTV	A5U4M0	246.2 Da LogP 2.40 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(cc1)C(=O)CC(=O)C(F)(F)F`

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
ZINC100034341 ZINC	1.000	246.2 Da LogP 2.40 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)C(F)(F)F)cc1`
ZINC100351835 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[P@@](=O)(O)OP(=O)(O)…`
ZINC104897282 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[P@](=O)(O)OP(=O)(O)O…`
ZINC13515641 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](O[P@@](=O)(O)OP(=O)(O)…`
ZINC154566 ZINC	1.000	257.2 Da LogP 2.83 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1C(=O)O`
ZINC2004372 ZINC	1.000	221.3 Da LogP 1.19 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCNC1CCCCC1`
ZINC255995137 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[P@](=O)(O)OP(=O)(O)O…`
ZINC255995138 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@@H]1O[C@H](O[P@](=O)(O)OP(=O)(O)O…`
ZINC8215630 ZINC	1.000	390.1 Da LogP -2.23 TPSA 229.7	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](O[P@@](=O)(O)OP(=O)(O)O…`
ZINC4247392 ZINC	0.952	348.4 Da LogP 4.57 TPSA 98.7	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1Nc1ccccc1C(=O)O`
ZINC38364153 ZINC	0.926	235.3 Da LogP 1.58 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCCCNC1CCCCC1`
ZINC154642 ZINC	0.870	213.2 Da LogP 3.13 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1`
ZINC1710230 ZINC	0.786	207.3 Da LogP 0.80 TPSA 66.4	✓ Ro5	✓ Clean	`O=S(=O)(O)CCNC1CCCCC1`
ZINC1875251926 ZINC	0.771	309.1 Da LogP -1.91 TPSA 182.9	✓ Ro5	✓ Clean	`[O][P@](=O)(O)O[C@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC2173765 ZINC	0.769	227.3 Da LogP 3.44 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccccc1Nc1ccccc1C(=O)O`
ZINC3148993 ZINC	0.769	247.7 Da LogP 3.78 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1Cl`
ZINC3609637 ZINC	0.769	228.3 Da LogP 2.71 TPSA 75.3	✓ Ro5	✓ Clean	`Nc1ccccc1Nc1ccccc1C(=O)O`
ZINC72662 ZINC	0.769	231.2 Da LogP 3.27 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1F`
ZINC100042039 ZINC	0.765	296.2 Da LogP 3.03 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)C(F)(F)C(F)(F)F)cc1`
ZINC100497170 ZINC	0.765	262.6 Da LogP 2.67 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)C(F)(F)Cl)cc1`
ZINC13522068 ZINC	0.765	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC3870205 ZINC	0.765	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@@H](O)[C…`
ZINC4095560 ZINC	0.765	310.1 Da LogP -2.35 TPSA 183.2	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC32314 ZINC	0.750	241.2 Da LogP 2.20 TPSA 80.4	✓ Ro5	Alert	`Nc1ccccc1C(=O)c1ccccc1C(=O)O`
ZINC12502703 ZINC	0.743	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@@H](OP(=O)(O)O)[C@H](O)[C@…`
ZINC4095589 ZINC	0.743	340.1 Da LogP -2.99 TPSA 203.4	1 viol.	✓ Clean	`O=P(O)(O)OC[C@H]1O[C@H](OP(=O)(O)O)[C@H](O)[C@@…`
ZINC21999422 ZINC	0.741	229.2 Da LogP 2.83 TPSA 69.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccc(O)cc1`
ZINC26897417 ZINC	0.741	289.3 Da LogP 4.80 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1-c1ccccc1`
ZINC3631865 ZINC	0.741	257.2 Da LogP 2.83 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)c1ccc(Nc2ccccc2C(=O)O)cc1`
ZINC3876604 ZINC	0.727	234.3 Da LogP 2.88 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)C(C)(C)C)cc1`
ZINC102895904 ZINC	0.724	354.2 Da LogP 3.10 TPSA 68.3	✓ Ro5	✓ Clean	`O=C(CC(=O)C(F)(F)F)c1ccc(C(=O)CC(=O)C(F)(F)F)cc1`
ZINC36294190 ZINC	0.724	231.2 Da LogP 2.77 TPSA 63.3	✓ Ro5	✓ Clean	`Nc1cc(-c2ccc(F)cc2)ccc1C(=O)O`
ZINC100041989 ZINC	0.722	346.2 Da LogP 3.67 TPSA 43.4	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)C(F)(F)C(F)(F)C(F)(F)F)cc1`
ZINC100068461 ZINC	0.714	260.2 Da LogP 2.79 TPSA 43.4	✓ Ro5	✓ Clean	`CCOc1ccc(C(=O)CC(=O)C(F)(F)F)cc1`
ZINC100718804 ZINC	0.714	274.2 Da LogP 3.18 TPSA 43.4	✓ Ro5	✓ Clean	`CC(C)Oc1ccc(C(=O)CC(=O)C(F)(F)F)cc1`
ZINC1606178 ZINC	0.714	292.1 Da LogP 3.89 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccc(Br)cc1`
ZINC16545049 ZINC	0.714	263.3 Da LogP 4.28 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1cccc2ccccc12`
ZINC1688663 ZINC	0.714	228.3 Da LogP 2.71 TPSA 75.3	✓ Ro5	Alert	`Nc1ccc(Nc2ccccc2C(=O)O)cc1`
ZINC26479899 ZINC	0.714	214.2 Da LogP 2.52 TPSA 62.2	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccncc1`
ZINC347210 ZINC	0.714	247.7 Da LogP 3.78 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccc(Cl)cc1`
ZINC403440 ZINC	0.714	231.2 Da LogP 3.27 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccc(F)cc1`
ZINC5160660 ZINC	0.714	227.3 Da LogP 3.44 TPSA 49.3	✓ Ro5	✓ Clean	`Cc1ccc(Nc2ccccc2C(=O)O)cc1`
ZINC575408789 ZINC	0.706	276.2 Da LogP 2.41 TPSA 52.6	✓ Ro5	✓ Clean	`COc1cc(OC)cc(C(=O)CC(=O)C(F)(F)F)c1`
ZINC36429 ZINC	0.700	284.3 Da LogP 3.16 TPSA 52.6	✓ Ro5	✓ Clean	`COc1ccc(C(=O)CC(=O)c2ccc(OC)cc2)cc1`
ZINC1183 ZINC	0.690	282.1 Da LogP 4.44 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1cccc(Cl)c1Cl`
ZINC1625 ZINC	0.690	291.7 Da LogP 3.48 TPSA 86.6	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1cc(Cl)ccc1C(=O)O`
ZINC2046924 ZINC	0.690	281.2 Da LogP 4.15 TPSA 49.3	✓ Ro5	✓ Clean	`O=C(O)c1ccccc1Nc1ccccc1C(F)(F)F`
ZINC21995266 ZINC	0.690	255.3 Da LogP 4.25 TPSA 49.3	✓ Ro5	✓ Clean	`CC(C)c1ccccc1Nc1ccccc1C(=O)O`
ZINC21995270 ZINC	0.690	269.3 Da LogP 4.43 TPSA 49.3	✓ Ro5	✓ Clean	`CC(C)(C)c1ccccc1Nc1ccccc1C(=O)O`
ZINC3173666 ZINC	0.690	243.3 Da LogP 3.14 TPSA 58.6	✓ Ro5	✓ Clean	`COc1ccccc1Nc1ccccc1C(=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.