Protein target profile

KP13_04181

Aspartate aminotransferase

Genome: KpKP13 Gene: AHE45412.1 aspC 3D evidence: AlphaFold DB model + ColabFold model UniProt A0A0H3GV21

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Length 396

Pocket druggability 0.431

Direct ligand evidence 0 90 total records

Functional annotation 1 EC 10 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

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Moderate predicted binding pocket FPocket selected-pocket score 0.43. This supports review but is not experimental validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.91. Structure available AlphaFold DB model + ColabFold model 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 (%): 42.748 Lower values reduce human off-target concern.
Human E-value: 6.22e-101
Gut microbiome similarity: 3.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 63.131 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: 96.61 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 0.431

Structure A0A0H3GV21

Pocket Pocket 6

P2Rank 0.913

Structure A0A0H3GV21

Pocket Pocket 1

ColabFold model

FPocket 0.412 · Pocket 5

P2Rank 0.87 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 174 / 4744 genomes with a hit

Prevalence 3.7%

Cross-references

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

Sequence

UniProt A0A0H3GV21

Chemistry

ChEMBL CHEMBL595

Sequence

Primary amino-acid sequence viewer.

MFENITAAPADPILGLADLFRADDRPEKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGNAIIADKRARTAQTPGGTGALRVAADFLAKNTDVKRVWVSNPSWPNHKSVFTSAGLEVREYAYYDAANHALDFDGLLASLNEAQAGDVVLFHGCCHNPTGIDPTLDQWQQLAQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAALHKELLVASSYSKNFGLYNERVGACTLVAADQETVDRAFSQMKSVIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQRIQRMRLLFVNTLQEKGASRDFSFISQQNGMFSFSGLTKEQVLRLREEFAIYAVASGRINVAGMTPDNMAPLCEAIVAVL

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

2.6.1.-

Gene Ontology (GO)

GO:0030170 Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6.
GO:0008483 Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0009058 A cellular process consisting of the biochemical pathways by which a living organism synthesizes chemical substances. This typically represents the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0042802 Binding to an identical protein or proteins.
GO:0004069 Catalysis of the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
GO:0004838 Catalysis of the reaction: L-tyrosine + 2-oxoglutarate = 3-(4-hydroxyphenyl)pyruvate + L-glutamate.
GO:0033585 OBSOLETE. The chemical reactions and pathways resulting in the formation of L-phenylalanine from other compounds, including chorismate, via the intermediate phenylpyruvate.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

23 records

Show feature table

Start	End	DB	Term	Name
27	392	Pfam	PF00155	Aminotransferase class I and II
27	392	InterPro	IPR004839	Aminotransferase, class I/classII
243	256	ProSitePatterns	PS00105	Aminotransferases class-I pyridoxal-phosphate attachment site.
243	256	InterPro	IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site
175	194	PRINTS	PR00799	Aspartate aminotransferase signature
175	194	InterPro	IPR000796	Aspartate/other aminotransferase
341	359	PRINTS	PR00799	Aspartate aminotransferase signature
341	359	InterPro	IPR000796	Aspartate/other aminotransferase
273	298	PRINTS	PR00799	Aspartate aminotransferase signature
273	298	InterPro	IPR000796	Aspartate/other aminotransferase
206	218	PRINTS	PR00799	Aspartate aminotransferase signature
206	218	InterPro	IPR000796	Aspartate/other aminotransferase
1	396	SUPERFAMILY	SSF53383	PLP-dependent transferases
1	396	InterPro	IPR015424	Pyridoxal phosphate-dependent transferase
5	392	Gene3D	G3DSA:3.90.1150.10	Aspartate Aminotransferase, domain 1
5	392	InterPro	IPR015422	Pyridoxal phosphate-dependent transferase, small domain
60	300	FunFam	G3DSA:3.40.640.10:FF:000015	Aspartate aminotransferase
60	300	Gene3D	G3DSA:3.40.640.10	-
60	300	InterPro	IPR015421	Pyridoxal phosphate-dependent transferase, major domain
29	392	CDD	cd00609	AAT_like
1	395	PANTHER	PTHR11879	ASPARTATE AMINOTRANSFERASE
1	395	InterPro	IPR000796	Aspartate/other aminotransferase
289	392	FunFam	G3DSA:3.90.1150.10:FF:000001	Aspartate aminotransferase

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

0.431

Likely same site as P2Rank 2 1.7 Å 11 shared residues 85% of smaller site

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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

0.913

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Surrounding area

Site 2 P2Rank #2

0.141

Likely same site as FPocket 6 1.7 Å 11 shared residues 85% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.03

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Surrounding area

Site 4 P2Rank #4

0.025

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Surrounding area

Site 5 P2Rank #5

0.018

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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

0.87

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Surrounding area

Site 2 P2Rank #2

0.172

Likely same site as FPocket 5 2.0 Å 14 shared residues 93% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.048

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Surrounding area

Site 4 P2Rank #4

0.034

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Surrounding area

Site 5 P2Rank #5

0.023

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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_A0A0H3GV21	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold KP13_04181	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.

90 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 40 records from similar proteins

Structural ligands 39 0 loaded crystals

Measured bioactivity 1 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0A0 PDB via homolog 147.1 Da · LogP -0.74 · TPSA 100.6 Open detail RCSB PDB

3IB PDB via homolog Detail RCSB PDB

3QP PDB via homolog Detail RCSB PDB

4TB PDB via homolog Detail RCSB PDB

5PV 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
0A0 RCSB PDB	1ART	P00509	147.1 Da LogP -0.74 TPSA 100.6	✓ Ro5	✓ Clean	`C[C@](CC(=O)O)(C(=O)O)N`
3IB RCSB PDB	2AY6	P95468	203.2 Da LogP 2.58 TPSA 53.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CCCC(=O)O`
3QP RCSB PDB	3QPG	P00509	361.2 Da LogP 0.66 TPSA 173.9	✓ Ro5	✓ Clean	`Cc1ccc(c(c1O)/C=N/[C@@H](CC(=O)O)C(=O)O)COP(=O)…`
4TB RCSB PDB	2AY8	P95468	170.2 Da LogP 2.16 TPSA 37.3	✓ Ro5	✓ Clean	`c1cc(sc1)CCCC(=O)O`
5PV RCSB PDB	2AY9	P95468	178.2 Da LogP 2.48 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CCCCC(=O)O`
77E RCSB PDB	5T4L	P00509	348.3 Da LogP 0.83 TPSA 163.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CC[C@H](CCC(=O)O)N)O`
AHC RCSB PDB	2AY1	P95468	165.2 Da LogP 1.29 TPSA 63.3	✓ Ro5	Alert	`c1cc(ccc1CCC(=O)O)N`
AKG RCSB PDB	1AIB	P00509	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
CLT RCSB PDB	2AY7	P95468	164.2 Da LogP 2.09 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CCCC(=O)O`
CXP RCSB PDB	2AY2	P95468	156.2 Da LogP 2.43 TPSA 37.3	✓ Ro5	✓ Clean	`C1CCC(CC1)CCC(=O)O`
GUA RCSB PDB	1AMS	P00509	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
HCI RCSB PDB	1AHX	P00509	150.2 Da LogP 1.70 TPSA 37.3	✓ Ro5	✓ Clean	`c1ccc(cc1)CCC(=O)O`
IOP RCSB PDB	1AHF	P00509	189.2 Da LogP 2.19 TPSA 53.1	✓ Ro5	✓ Clean	`c1ccc2c(c1)c(c[nH]2)CCC(=O)O`
IVA RCSB PDB	1YOO	P00509	102.1 Da LogP 1.12 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CC(=O)O`
KET RCSB PDB	4RKD	C7E5X4	363.2 Da LogP -0.53 TPSA 188.1	✓ Ro5	✓ Clean	`Cc1c(c(c(c[nH+]1)COP(=O)(O)O)C=NC(CC(=O)O)C(=O)…`
KYN RCSB PDB	3PD6	P05202	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`c1ccc(c(c1)C(=O)C[C@@H](C(=O)O)N)N`
LMR RCSB PDB	6T3V	C7E5X4	134.1 Da LogP -1.09 TPSA 94.8	✓ Ro5	✓ Clean	`C([C@@H](C(=O)O)O)C(=O)O`
MAE RCSB PDB	1AHY	P00509	116.1 Da LogP -0.29 TPSA 74.6	✓ Ro5	✓ Clean	`C(=C/C(=O)O)/C(=O)O`
MPL RCSB PDB	1ASD	P00509	262.2 Da LogP -0.05 TPSA 107.9	✓ Ro5	✓ Clean	`Cc1c(c(c(c[n+]1C)COP(=O)(O)O)C=O)O`
MPP RCSB PDB	2AY3	P95468	210.2 Da LogP 1.72 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(cc1OC)CCC(=O)O`
NOP RCSB PDB	1ASE	P00509	263.1 Da LogP -0.24 TPSA 131.0	✓ Ro5	✓ Clean	`Cc1c(c(c(c[n+]1[O-])COP(=O)(O)O)C=O)O`
NPL RCSB PDB	1ASC	P00509	263.2 Da LogP -0.41 TPSA 116.9	✓ Ro5	✓ Clean	`Cc1c(c(c(c[n+]1C)COP(=O)(O)O)CN)O`
OAA RCSB PDB	3PDB	P05202	131.1 Da LogP -2.22 TPSA 94.5	✓ Ro5	✓ Clean	`C(C(=O)C(=O)O)C(=O)[O-]`
PDG RCSB PDB	1X2A	P00509	378.3 Da LogP 0.11 TPSA 186.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@H](CCC(=O)O)C(=O)…`
PGU RCSB PDB	1X28	P00509	378.3 Da LogP 0.11 TPSA 186.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)C(=O…`
PJ7 RCSB PDB	3PA9	D3H0F7	127.1 Da LogP 0.56 TPSA 76.5	✓ Ro5	✓ Clean	`c1c(coc1C(=O)O)N`
PL6 RCSB PDB	5VWR	P00509	376.3 Da LogP 0.44 TPSA 186.8	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)\C=N\[C@@H](CCC(=O)O)C…`
PLA RCSB PDB	1ASL	P00509	378.3 Da LogP 0.11 TPSA 186.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@](C)(CC(=O)O)C(=…`
PLR RCSB PDB	3FSL	P04693	233.2 Da LogP 1.01 TPSA 99.9	✓ Ro5	✓ Clean	`Cc1c(cnc(c1O)C)COP(=O)(O)O`
PMG RCSB PDB	1X29	P00509	392.3 Da LogP 0.50 TPSA 186.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@](C)(CCC(=O)O)C(…`
PMP RCSB PDB	1AIA	P00509	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
PP3 RCSB PDB	1C9C	P00509	320.2 Da LogP 0.27 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](C)C(=O)O)O`
PPD RCSB PDB	1ARG	P00509	364.2 Da LogP -0.28 TPSA 186.5	1 viol.	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CC(=O)O)C(=O)…`
PPT RCSB PDB	2AY4	P95468	164.2 Da LogP 2.01 TPSA 37.3	✓ Ro5	✓ Clean	`Cc1ccc(cc1)CCC(=O)O`
PSZ RCSB PDB	2QBT	P00509	374.3 Da LogP 2.08 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cc(sc2)C(=O)O)O`
PY4 RCSB PDB	1CQ6	P00509	334.3 Da LogP 0.66 TPSA 149.2	✓ Ro5	✓ Clean	`CC[C@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O`
PY5 RCSB PDB	1CQ7	P00509	348.3 Da LogP 1.05 TPSA 149.2	✓ Ro5	✓ Clean	`CCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O`
PY6 RCSB PDB	1CQ8	P00509	362.3 Da LogP 1.44 TPSA 149.2	✓ Ro5	✓ Clean	`CCCC[C@@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O`
SIN RCSB PDB	1CZE	P00509	118.1 Da LogP -0.06 TPSA 74.6	✓ Ro5	✓ Clean	`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
CHEMBL595 ChEMBL	P00507	—	356.4 Da LogP 3.16 TPSA 68.3	✓ Ro5	✓ Clean	`CCc1ccc(CCOc2ccc(CC3SC(=O)NC3=O)cc2)nc1`

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`
ZINC895186 ZINC	1.000	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)C[C@H](N)C(=O)O`
ZINC901103 ZINC	1.000	208.2 Da LogP 0.25 TPSA 106.4	✓ Ro5	✓ Clean	`Nc1ccccc1C(=O)C[C@@H](N)C(=O)O`
ZINC968326 ZINC	1.000	356.4 Da LogP 3.16 TPSA 68.3	✓ Ro5	✓ Clean	`CCc1ccc(CCOc2ccc(C[C@@H]3SC(=O)NC3=O)cc2)nc1`
ZINC968327 ZINC	1.000	356.4 Da LogP 3.16 TPSA 68.3	✓ Ro5	✓ Clean	`CCc1ccc(CCOc2ccc(C[C@H]3SC(=O)NC3=O)cc2)nc1`
ZINC57378 ZINC	0.818	203.2 Da LogP 2.58 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)CCCc1c[nH]c2ccccc12`
ZINC156029 ZINC	0.813	224.3 Da LogP 2.11 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(CCCC(=O)O)cc1OC`
ZINC16696671 ZINC	0.800	355.5 Da LogP 2.97 TPSA 75.1	✓ Ro5	✓ Clean	`CCc1ccc(CCOc2ccc(C[C@@H]3SC(=N)NC3=O)cc2)nc1`
ZINC16696673 ZINC	0.800	355.5 Da LogP 2.97 TPSA 75.1	✓ Ro5	✓ Clean	`CCc1ccc(CCOc2ccc(C[C@H]3SC(=N)NC3=O)cc2)nc1`
ZINC406914 ZINC	0.800	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(CCC(=O)O)cc1`
ZINC44699637 ZINC	0.796	372.4 Da LogP 2.13 TPSA 88.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@@H](Cc2ccc(OCCc3ccc(CCO)cn3)cc2)S1`
ZINC44699639 ZINC	0.796	372.4 Da LogP 2.13 TPSA 88.5	✓ Ro5	✓ Clean	`O=C1NC(=O)[C@H](Cc2ccc(OCCc3ccc(CCO)cn3)cc2)S1`
ZINC11885676 ZINC	0.794	224.3 Da LogP 2.11 TPSA 55.8	✓ Ro5	✓ Clean	`CCOc1cc(CCC(=O)O)ccc1OC`
ZINC2566960 ZINC	0.794	231.3 Da LogP 3.36 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCc1c[nH]c2ccccc12`
ZINC37632578 ZINC	0.794	217.3 Da LogP 2.97 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)CCCCc1c[nH]c2ccccc12`
ZINC37632580 ZINC	0.794	245.3 Da LogP 3.75 TPSA 53.1	✓ Ro5	✓ Clean	`O=C(O)CCCCCCc1c[nH]c2ccccc12`
ZINC8019344 ZINC	0.794	224.3 Da LogP 2.11 TPSA 55.8	✓ Ro5	✓ Clean	`CCOc1ccc(CCC(=O)O)cc1OC`
ZINC1678807 ZINC	0.788	238.3 Da LogP 2.50 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(CCCCC(=O)O)cc1OC`
ZINC1703342 ZINC	0.786	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC2575989 ZINC	0.778	253.3 Da LogP 0.58 TPSA 98.8	✓ Ro5	✓ Clean	`COc1cc(CCC(=O)O)ccc1OCC(N)=O`
ZINC8019416 ZINC	0.771	238.3 Da LogP 2.50 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(CCC(=O)O)ccc1OC(C)C`
ZINC1529497 ZINC	0.769	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045 ZINC	0.769	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=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`
ZINC1593115 ZINC	0.769	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020 ZINC	0.769	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440 ZINC	0.769	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298 ZINC	0.769	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062 ZINC	0.769	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC1482946 ZINC	0.765	370.4 Da LogP 2.80 TPSA 85.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCOc2ccc(C[C@H]3SC(=O)NC3=O)cc2)nc1`
ZINC1482949 ZINC	0.765	386.4 Da LogP 2.22 TPSA 105.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(CCOc2ccc(C[C@@H]3SC(=O)NC3=O)cc2)n…`
ZINC3784663 ZINC	0.765	370.4 Da LogP 2.80 TPSA 85.4	✓ Ro5	✓ Clean	`CC(=O)c1ccc(CCOc2ccc(C[C@@H]3SC(=O)NC3=O)cc2)nc1`
ZINC3784710 ZINC	0.765	386.4 Da LogP 2.22 TPSA 105.6	✓ Ro5	✓ Clean	`O=C(O)Cc1ccc(CCOc2ccc(C[C@H]3SC(=O)NC3=O)cc2)nc1`
ZINC454762 ZINC	0.750	209.2 Da LogP 1.12 TPSA 61.5	✓ Ro5	✓ Clean	`COc1ccc(CCC(N)=O)cc1OC`
ZINC71867277 ZINC	0.750	246.2 Da LogP 2.31 TPSA 55.8	✓ Ro5	✓ Clean	`COc1cc(CCC(=O)O)ccc1OC(F)F`
ZINC77291743 ZINC	0.750	276.3 Da LogP 0.89 TPSA 110.1	✓ Ro5	✓ Clean	`COc1ccc(CCC(=O)O)cc1OS(=O)(=O)O`
ZINC91252013 ZINC	0.750	264.2 Da LogP 2.61 TPSA 55.8	✓ Ro5	✓ Clean	`COc1ccc(CCC(=O)O)cc1OC(F)(F)F`
ZINC9998612 ZINC	0.750	226.3 Da LogP 3.37 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCc1ccc(-c2ccccc2)cc1`
ZINC517260 ZINC	0.743	249.3 Da LogP 3.98 TPSA 32.9	✓ Ro5	✓ Clean	`O=C(CCc1c[nH]c2ccccc12)c1ccccc1`
ZINC2163727 ZINC	0.739	222.2 Da LogP 1.72 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCc1cccc(CCC(=O)O)c1`
ZINC1482947 ZINC	0.736	372.4 Da LogP 2.65 TPSA 88.5	✓ Ro5	✓ Clean	`C[C@@H](O)c1ccc(CCOc2ccc(C[C@H]3SC(=O)NC3=O)cc2…`
ZINC3784667 ZINC	0.736	372.4 Da LogP 2.65 TPSA 88.5	✓ Ro5	✓ Clean	`C[C@@H](O)c1ccc(CCOc2ccc(C[C@@H]3SC(=O)NC3=O)cc…`
ZINC6713959 ZINC	0.736	372.4 Da LogP 2.65 TPSA 88.5	✓ Ro5	✓ Clean	`C[C@H](O)c1ccc(CCOc2ccc(C[C@H]3SC(=O)NC3=O)cc2)…`
ZINC6713967 ZINC	0.736	372.4 Da LogP 2.65 TPSA 88.5	✓ Ro5	✓ Clean	`C[C@H](O)c1ccc(CCOc2ccc(C[C@@H]3SC(=O)NC3=O)cc2…`
ZINC82292866 ZINC	0.730	232.3 Da LogP 1.77 TPSA 65.1	✓ Ro5	✓ Clean	`O=C(O)CCNCCc1c[nH]c2ccccc12`
ZINC1673354 ZINC	0.727	238.3 Da LogP 3.82 TPSA 17.1	✓ Ro5	✓ Clean	`O=C(CCc1ccccc1)CCc1ccccc1`
ZINC1693912 ZINC	0.727	266.3 Da LogP 3.39 TPSA 34.1	✓ Ro5	Alert	`O=C(CCc1ccccc1)C(=O)CCc1ccccc1`
ZINC22063071 ZINC	0.727	224.3 Da LogP 1.81 TPSA 44.8	✓ Ro5	✓ Clean	`COC(=O)CCc1ccc(OC)c(OC)c1`
ZINC2633246 ZINC	0.722	325.4 Da LogP 1.50 TPSA 96.3	✓ Ro5	✓ Clean	`COc1ccc(CCN(CCC(=O)O)CCC(=O)O)cc1OC`
ZINC79036547 ZINC	0.719	209.2 Da LogP 0.38 TPSA 100.6	✓ Ro5	✓ Clean	`N[C@H](CC(=O)c1ccccc1O)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.