Protein target profile

KP13_00092

2-aminoethylphosphonate--pyruvate transaminase

Genome: KpKP13 Gene: phnW AHE42017.1 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GYY8

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Length 367

Pocket druggability 0.379

Direct ligand evidence 0 77 total records

Functional annotation 1 EC 3 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.

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 7 structural and 20 bioactivity records.

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 (%): 25.625 Lower values reduce human off-target concern.
Human E-value: 1.2e-20
Gut microbiome similarity: 8.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 65.746 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: 97.3 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 0.379

Structure A0A0H3GYY8

Pocket Pocket 1

P2Rank 0.334

Structure A0A0H3GYY8

Pocket Pocket 1

ColabFold model

FPocket 0.218 · Pocket 2

P2Rank 0.44 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 389 / 4744 genomes with a hit

Prevalence 8.2%

Cross-references

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

Sequence

UniProt A0A0H3GYY8

Chemistry

ChEMBL CHEMBL5170947 ChEMBL CHEMBL5207596 ChEMBL CHEMBL3764222 ChEMBL CHEMBL3763469 ChEMBL CHEMBL3764023 ChEMBL CHEMBL3764351 ChEMBL CHEMBL3765396 ChEMBL CHEMBL5181500 ChEMBL CHEMBL5179589 ChEMBL CHEMBL3763498 ChEMBL CHEMBL5207995 ChEMBL CHEMBL5204588 ChEMBL CHEMBL5183689 ChEMBL CHEMBL3765186 ChEMBL CHEMBL5199538 ChEMBL CHEMBL5173536 ChEMBL CHEMBL5195123 ChEMBL CHEMBL3765807 ChEMBL CHEMBL5189330 ChEMBL CHEMBL4744771

Sequence

Primary amino-acid sequence viewer.

MTSRNYLLLTPGPLTTSRTVKEAMLFDSCTWDDDYNLGVVQTIRQQLVQLATPADGYTAVLLQGSGSYAVEAVLGSVIGEQGKVLIVSNGAYGARMIEMAQLMGIACHPYDCGEVSRPDAAAIEQILQNDPAITHIAMVHSETTTGMLNPIAEVAELAKRYDKRYIVDAMSSFGGIPLDIAALNIDYLISSANKCIQGVPGFAFVIAREAELAACKGRSRSLSLDLYAQWRCMEDNHGKWRFTSPTHTVLAFAQALKELAQEGGVSARHQRYRNNQRRLVAGMRALGFRPLLDDSLHSPIITAFYSPDAPQYRFHTFYQKLKDQGFVIYPGKVSQSDCFRIGNIGEVYDADITALLAAIDNAMYWKQ

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

2.6.1.37

Gene Ontology (GO)

GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0019700 The chemical reactions and pathways resulting in the breakdown of phosphonates, any organic compound containing one or more C-PO(OH)2 or C-PO(OR)2 (with R=alkyl, aryl) groups. Catabolism of phosphonic acid itself, an inorganic compound without the biochemically relevant C-P bond, is not included.
GO:0047304 Catalysis of the reaction: (2-aminoethyl)phosphonate + pyruvate = L-alanine + phosphonoacetaldehyde.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
1	367	Hamap	MF_01376	2-aminoethylphosphonate--pyruvate transaminase [phnW].
1	367	InterPro	IPR012703	2-aminoethylphosphonate--pyruvate transaminase
9	354	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
9	354	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
40	302	Pfam	PF00266	Aminotransferase class-V
40	302	InterPro	IPR000192	Aminotransferase class V domain
4	366	NCBIfam	TIGR02326	2-aminoethylphosphonate--pyruvate transaminase
4	366	InterPro	IPR012703	2-aminoethylphosphonate--pyruvate transaminase
17	262	Gene3D	G3DSA:3.40.640.10	-
17	262	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
1	365	PIRSF	PIRSF000524	SPT
1	365	InterPro	IPR024169	Serine-pyruvate aminotransferase/2-aminoethylphosphonate-pyruvate transaminase
2	366	PANTHER	PTHR42778	2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE
7	363	NCBIfam	TIGR03301	2-aminoethylphosphonate aminotransferase
7	363	InterPro	IPR012703	2-aminoethylphosphonate--pyruvate transaminase
6	363	SUPERFAMILY	SSF53383	PLP-dependent transferases
6	363	InterPro	IPR015424	Pyridoxal phosphate-dependent 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 · FPocket

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

Site 1 FPocket #1

0.379

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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

0.334

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Surrounding area

Site 2 P2Rank #2

0.024

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Surrounding area

Site 3 P2Rank #3

0.008

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Surrounding area

Site 4 P2Rank #4

0.004

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Surrounding area

Residue sets

UniProt: Binding site:340-340

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.44

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Surrounding area

Site 2 P2Rank #2

0.061

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Surrounding area

Site 3 P2Rank #3

0.021

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Surrounding area

Site 4 P2Rank #4

0.02

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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_A0A0H3GYY8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_00092	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.

77 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 27 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 20 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

AOA PDB via homolog 91.1 Da · LogP -1.04 · TPSA 72.5 Open detail RCSB PDB

BTB PDB via homolog Detail RCSB PDB

KY1 PDB via homolog Detail RCSB PDB

MMM PDB via homolog Detail RCSB PDB

PLR 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
AOA RCSB PDB	1H0C	P21549	91.1 Da LogP -1.04 TPSA 72.5	✓ Ro5	✓ Clean	`C(C(=O)O)ON`
BTB RCSB PDB	2YOB	P21549	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`C(CO)N(CCO)C(CO)(CO)CO`
KY1 RCSB PDB	2CH2	Q7PRG3	193.2 Da LogP 1.32 TPSA 80.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)CCC(=O)O)N`
MMM RCSB PDB	2YRI	Q5SLX0	348.2 Da LogP -0.04 TPSA 169.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@](C)(CO)C(=O)…`
PLR RCSB PDB	5HHY	P21549	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1c(cnc(c1O)C)COP(=O)(O)O`
PMP RCSB PDB	6RV0	P21549	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
POA RCSB PDB	1M32	P96060	124.0 Da LogP -0.64 TPSA 74.6	✓ Ro5	✓ Clean	`C(C=O)P(=O)(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
CHEMBL5170947 ChEMBL	P21549	8.70 ~2.0 nM	209.7 Da LogP 2.56 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NCOc1ccc2ccccc2c1`
CHEMBL5207596 ChEMBL	P21549	7.57 ~26.9 nM	199.3 Da LogP 2.74 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1cccc(-c2ccccc2)c1`
CHEMBL3764222 ChEMBL	P21549	7.40 ~39.8 nM	189.6 Da LogP 1.51 TPSA 44.5	✓ Ro5	✓ Clean	`COc1cccc(CON)c1.Cl`
CHEMBL3763469 ChEMBL	P21549	7.30 ~50.1 nM	238.5 Da LogP 2.26 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1cccc(Br)c1`
CHEMBL3764023 ChEMBL	P21549	7.22 ~60.3 nM	194.1 Da LogP 2.15 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1ccc(Cl)cc1`
CHEMBL3764351 ChEMBL	P21549	7.10 ~79.4 nM	189.6 Da LogP 1.51 TPSA 44.5	✓ Ro5	✓ Clean	`COc1ccc(CON)cc1.Cl`
CHEMBL3765396 ChEMBL	P21549	7.07 ~85.1 nM	177.6 Da LogP 1.64 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1ccc(F)cc1`
CHEMBL5181500 ChEMBL	P21549	6.96 ~109.6 nM	179.2 Da LogP 2.29 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1cc2ccccc2s1`
CHEMBL5179589 ChEMBL	P21549	6.80 ~158.5 nM	173.6 Da LogP 1.81 TPSA 35.2	✓ Ro5	✓ Clean	`Cc1ccc(CON)cc1.Cl`
CHEMBL3763498 ChEMBL	P21549	6.70 ~199.5 nM	235.7 Da LogP 3.17 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1ccc(-c2ccccc2)cc1`
CHEMBL5207995 ChEMBL	P21549	6.64 ~229.1 nM	163.2 Da LogP 1.82 TPSA 48.4	✓ Ro5	✓ Clean	`NOCc1cc2ccccc2o1`
CHEMBL5204588 ChEMBL	P21549	6.62 ~239.9 nM	192.3 Da LogP 1.68 TPSA 38.5	✓ Ro5	✓ Clean	`NOCc1cccc(N2CCCC2)c1`
CHEMBL5183689 ChEMBL	P21549	6.55 ~281.8 nM	217.2 Da LogP 2.88 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1cccc(-c2ccc(F)cc2)c1`
CHEMBL3765186 ChEMBL	P21549	6.52 ~302.0 nM	195.6 Da LogP 1.78 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1ccc(F)cc1F`
CHEMBL5199538 ChEMBL	P21549	6.26 ~549.5 nM	267.2 Da LogP 3.76 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1cccc(-c2ccc(C(F)(F)F)cc2)c1`
CHEMBL5173536 ChEMBL	P21549	6.22 ~602.6 nM	159.6 Da LogP 1.50 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1ccccc1`
CHEMBL5195123 ChEMBL	P21549	6.21 ~616.6 nM	182.2 Da LogP 1.10 TPSA 57.4	✓ Ro5	✓ Clean	`COc1c(C)cnc(CON)c1C`
CHEMBL3765807 ChEMBL	P21549	6.16 ~691.8 nM	194.1 Da LogP 2.15 TPSA 35.2	✓ Ro5	✓ Clean	`Cl.NOCc1cccc(Cl)c1`
CHEMBL5189330 ChEMBL	P21549	6.07 ~851.1 nM	208.3 Da LogP 0.91 TPSA 47.7	✓ Ro5	✓ Clean	`NOCc1cccc(N2CCOCC2)c1`
CHEMBL4744771 ChEMBL	Q0IG34	—	240.2 Da LogP -2.58 TPSA 79.0	✓ Ro5	✓ Clean	`O=C([O-])CCc1nc(-c2ccccc2)no1.[Na+]`

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
ZINC1532708 ZINC	1.000	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC1615342 ZINC	1.000	209.2 Da LogP -3.01 TPSA 104.4	✓ Ro5	✓ Clean	`OCCN(CCO)C(CO)(CO)CO`
ZINC4105160 ZINC	0.958	202.1 Da LogP 1.84 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1cccc(Br)c1`
ZINC13356583 ZINC	0.821	207.2 Da LogP 1.71 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)CCCC(=O)O`
ZINC1532705 ZINC	0.769	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC2437734 ZINC	0.757	218.2 Da LogP 1.75 TPSA 76.2	✓ Ro5	✓ Clean	`O=C(O)CCc1nc(-c2ccccc2)no1`
ZINC2354961 ZINC	0.718	217.2 Da LogP 1.15 TPSA 82.0	✓ Ro5	✓ Clean	`NC(=O)CCc1nc(-c2ccccc2)no1`
ZINC1656021 ZINC	0.692	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C)c1O`
ZINC38070891 ZINC	0.686	251.3 Da LogP 3.83 TPSA 26.0	✓ Ro5	✓ Clean	`NCc1cccc(-c2ccc(C(F)(F)F)cc2)c1`
ZINC4384083 ZINC	0.683	231.3 Da LogP 1.42 TPSA 68.0	✓ Ro5	✓ Clean	`CNC(=O)CCc1nc(-c2ccccc2)no1`
ZINC1754752 ZINC	0.680	229.3 Da LogP 2.66 TPSA 44.5	✓ Ro5	✓ Clean	`NOCc1ccc(OCc2ccccc2)cc1`
ZINC1612530 ZINC	0.677	225.3 Da LogP 3.08 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)CCc1ccccc1`
ZINC2357513 ZINC	0.675	232.2 Da LogP 2.14 TPSA 76.2	✓ Ro5	✓ Clean	`O=C(O)CCCc1nc(-c2ccccc2)no1`
ZINC12958705 ZINC	0.667	209.2 Da LogP 1.77 TPSA 48.4	✓ Ro5	✓ Clean	`COc1c(C)cnc(COC(C)=O)c1C`
ZINC2567379 ZINC	0.667	257.1 Da LogP 2.50 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)c1ccccc1Br`
ZINC33749581 ZINC	0.667	245.3 Da LogP 1.76 TPSA 59.2	✓ Ro5	✓ Clean	`CN(C)C(=O)CCc1nc(-c2ccccc2)no1`
ZINC2353384 ZINC	0.659	231.3 Da LogP 1.54 TPSA 82.0	✓ Ro5	✓ Clean	`NC(=O)CCCc1nc(-c2ccccc2)no1`
ZINC32285266 ZINC	0.657	318.3 Da LogP 3.57 TPSA 77.8	✓ Ro5	✓ Clean	`c1ccc(-c2noc(CCc3nc(-c4ccccc4)no3)n2)cc1`
ZINC5763215 ZINC	0.656	201.2 Da LogP 2.95 TPSA 26.0	✓ Ro5	✓ Clean	`NCc1cccc(-c2ccc(F)cc2)c1`
ZINC11569614 ZINC	0.655	201.3 Da LogP 2.57 TPSA 35.2	✓ Ro5	✓ Clean	`NCCCOc1ccc2ccccc2c1`
ZINC6786083 ZINC	0.651	293.3 Da LogP 3.31 TPSA 68.0	✓ Ro5	✓ Clean	`O=C(CCc1nc(-c2ccccc2)no1)Nc1ccccc1`
ZINC32010384 ZINC	0.647	204.3 Da LogP 2.53 TPSA 29.3	✓ Ro5	✓ Clean	`NCc1cccc(N2CCCCCC2)c1`
ZINC1532514 ZINC	0.643	247.1 Da LogP 0.52 TPSA 117.0	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(C=O)c1O`
ZINC1680806 ZINC	0.640	258.3 Da LogP 3.42 TPSA 27.7	✓ Ro5	✓ Clean	`COc1ccc(COCc2ccc(OC)cc2)cc1`
ZINC4204306 ZINC	0.639	252.2 Da LogP 3.86 TPSA 20.2	✓ Ro5	✓ Clean	`OCc1cccc(-c2ccc(C(F)(F)F)cc2)c1`
ZINC34352328 ZINC	0.636	207.2 Da LogP 1.40 TPSA 69.4	✓ Ro5	✓ Clean	`COC(=O)CCC(=O)c1ccccc1N`
ZINC4384086 ZINC	0.636	245.3 Da LogP 1.81 TPSA 68.0	✓ Ro5	✓ Clean	`CCNC(=O)CCc1nc(-c2ccccc2)no1`
ZINC2518017 ZINC	0.633	212.6 Da LogP 2.39 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)c1ccccc1Cl`
ZINC86335427 ZINC	0.633	220.0 Da LogP 1.98 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1ccc(Br)cc1F`
ZINC86335654 ZINC	0.633	220.0 Da LogP 1.98 TPSA 35.2	✓ Ro5	✓ Clean	`NOCc1ccc(F)cc1Br`
ZINC2537758 ZINC	0.632	204.2 Da LogP 1.36 TPSA 76.2	✓ Ro5	✓ Clean	`O=C(O)Cc1nc(-c2ccccc2)no1`
ZINC2080743087 ZINC	0.625	200.2 Da LogP 2.14 TPSA 48.1	✓ Ro5	✓ Clean	`NOCc1cncc(-c2ccccc2)c1`
ZINC70236543 ZINC	0.625	214.3 Da LogP 3.27 TPSA 18.5	✓ Ro5	✓ Clean	`COc1cccc(COc2ccccc2)c1`
ZINC78276883 ZINC	0.625	228.3 Da LogP 3.41 TPSA 18.5	✓ Ro5	✓ Clean	`COc1cccc(COCc2ccccc2)c1`
ZINC2390188 ZINC	0.622	271.3 Da LogP 2.29 TPSA 59.2	✓ Ro5	✓ Clean	`O=C(CCc1nc(-c2ccccc2)no1)N1CCCC1`
ZINC2429784 ZINC	0.622	273.3 Da LogP 2.58 TPSA 68.0	✓ Ro5	✓ Clean	`CC(C)(C)NC(=O)CCc1nc(-c2ccccc2)no1`
ZINC2440872 ZINC	0.622	307.4 Da LogP 2.99 TPSA 68.0	✓ Ro5	✓ Clean	`O=C(CCc1nc(-c2ccccc2)no1)NCc1ccccc1`
ZINC4384095 ZINC	0.622	259.3 Da LogP 2.19 TPSA 68.0	✓ Ro5	✓ Clean	`CC(C)NC(=O)CCc1nc(-c2ccccc2)no1`
ZINC28278323 ZINC	0.621	201.1 Da LogP 2.60 TPSA 9.2	✓ Ro5	✓ Clean	`COCc1cccc(Br)c1`
ZINC399599 ZINC	0.621	242.3 Da LogP 3.49 TPSA 18.5	✓ Ro5	✓ Clean	`COc1cccc(CCc2cccc(OC)c2)c1`
ZINC1616708 ZINC	0.618	269.3 Da LogP 2.78 TPSA 80.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)CCc1ccccc1C(=O)O`
ZINC5064199 ZINC	0.615	244.3 Da LogP 3.28 TPSA 27.7	✓ Ro5	✓ Clean	`COc1ccc(COc2ccc(OC)cc2)cc1`
ZINC4434097 ZINC	0.614	245.3 Da LogP 1.81 TPSA 68.0	✓ Ro5	✓ Clean	`CNC(=O)CCCc1nc(-c2ccccc2)no1`
ZINC1059491 ZINC	0.613	211.3 Da LogP 2.69 TPSA 43.1	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)Cc1ccccc1`
ZINC2579878 ZINC	0.613	304.1 Da LogP 2.34 TPSA 54.4	✓ Ro5	✓ Clean	`O=C(O)CCC(=O)c1ccccc1I`
ZINC2114966 ZINC	0.610	332.2 Da LogP 0.99 TPSA 149.5	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(/C=N/CCCC(=O)O)c1O`
ZINC2332717 ZINC	0.609	321.4 Da LogP 3.03 TPSA 68.0	✓ Ro5	✓ Clean	`O=C(CCc1nc(-c2ccccc2)no1)NCCc1ccccc1`
ZINC37594000 ZINC	0.609	226.3 Da LogP 4.02 TPSA 9.2	✓ Ro5	✓ Clean	`Cc1ccc(COCc2ccc(C)cc2)cc1`
ZINC40543940 ZINC	0.609	295.3 Da LogP 0.74 TPSA 102.2	✓ Ro5	✓ Clean	`CS(=O)(=O)NC(=O)CCc1nc(-c2ccccc2)no1`
ZINC5561092 ZINC	0.609	285.3 Da LogP 2.68 TPSA 59.2	✓ Ro5	✓ Clean	`O=C(CCc1nc(-c2ccccc2)no1)N1CCCCC1`

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.