KpATCC43816 Protein target profile

branched-chain amino acid aminotransferase

Accession: VK055_3206

Gene: AIK81774.1 ilvE 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GPS2

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Length 309

Pocket druggability (P2Rank · AlphaFold DB model) 0.916

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 61 total records

Functional annotation 1 EC 11 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 93.3% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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: Hit
Human identity (%): 28.571 Lower values reduce human off-target concern.
Human E-value: 5.99e-20
Gut microbiome similarity: 4.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 44.518 Higher values support similarity to known essential genes.
DEG E-value: 3.34e-87 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 95.83 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) 0.916

Structure A0A0H3GPS2

Pocket Pocket 1

Druggability (FPocket) 0.683

Structure A0A0H3GPS2

Pocket Pocket 4

ColabFold model

P2Rank 0.883 · Pocket 1

FPocket 0.654 · Pocket 4

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 210 / 4744 genomes with a hit

Prevalence 4.4%

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 Glucosinolate biosynthesis, no isoenzyme backup detected, more central than 93.3% of genes in this genome.

Relative network centrality 93.3% more central than 93.3% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MTTKKADYIWFNGEMVPWGEAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLHDSAKIYRFPVSQSVDELMEACREVIRTNNLTSAYIRPLVFVGDVGMGVNPPPGYNTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKDLGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGAGRRGPVTKRIQEAFFGLFTGETEDKWGWLDPVSK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

2.6.1.42

Gene Ontology (GO)

GO:0009081 The chemical reactions and pathways involving amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
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:0004084 Catalysis of the reaction: a branched-chain amino acid (L-leucine, L-isoleucine and L-valine) + 2-oxoglutarate = L-glutamate + a 2-oxocarboxylate derived from the branched-chain amino acid.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0052656 Catalysis of the reaction: L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
GO:0052654 Catalysis of the reaction:L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
GO:0052655 Catalysis of the reaction: L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.
GO:0006532 The chemical reactions and pathways resulting in the formation of aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
GO:0009097 OBSOLETE. The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
GO:0009098 The chemical reactions and pathways resulting in the formation of L-leucine, 2-amino-4-methylpentanoic acid.
GO:0009099 The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

17 records

Show feature table

Start	End	DB	Term	Name
138	289	Gene3D	G3DSA:3.20.10.10	-
138	289	InterPro	IPR043132	Branched-chain-amino-acid aminotransferase-like, C-terminal
10	127	Gene3D	G3DSA:3.30.470.10	-
10	127	InterPro	IPR043131	Branched-chain-amino-acid aminotransferase-like, N-terminal
10	307	NCBIfam	TIGR01122	branched-chain-amino-acid transaminase
10	307	InterPro	IPR005785	Branched-chain amino acid aminotransferase I
194	223	ProSitePatterns	PS00770	Aminotransferases class-IV signature.
194	223	InterPro	IPR018300	Aminotransferase, class IV, conserved site
6	291	PANTHER	PTHR42743	AMINO-ACID AMINOTRANSFERASE
36	268	Pfam	PF01063	Amino-transferase class IV
36	268	InterPro	IPR001544	Aminotransferase class IV
10	127	FunFam	G3DSA:3.30.470.10:FF:000001	Branched-chain-amino-acid aminotransferase
22	295	CDD	cd01557	BCAT_beta_family
22	295	InterPro	IPR033939	Branched-chain aminotransferase
138	289	FunFam	G3DSA:3.20.10.10:FF:000001	Branched-chain-amino-acid aminotransferase
7	307	SUPERFAMILY	SSF56752	D-aminoacid aminotransferase-like PLP-dependent enzymes
7	307	InterPro	IPR036038	Aminotransferase-like, PLP-dependent enzymes

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

0.916

Likely same site as FPocket 1 1.6 Å 29 shared residues 91% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.461

Likely same site as FPocket 4 2.2 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.077

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Surrounding area

Pocket 4 P2Rank #4

0.023

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Surrounding area

Pocket 5 P2Rank #5

0.015

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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 #4

0.683

Likely same site as P2Rank 2 2.2 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.589 Unusual size

Likely same site as P2Rank 1 1.6 Å 29 shared residues 91% of smaller site

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Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.883

Likely same site as FPocket 1 3.0 Å 22 shared residues 96% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.208

Likely same site as FPocket 4 3.3 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.159

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Surrounding area

Pocket 4 P2Rank #4

0.059

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Surrounding area

Pocket 5 P2Rank #5

0.037

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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 #4

0.654

Likely same site as P2Rank 2 3.3 Å 9 shared residues 82% of smaller site

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Surrounding area

Pocket 2 FPocket #1

0.316 Unusual size

Likely same site as P2Rank 1 3.0 Å 22 shared residues 96% of smaller site

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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_A0A0H3GPS2	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_3206	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.

61 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 11 records from similar proteins

Structural ligands 11 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2ML PDB via homolog 145.2 Da · LogP 0.83 · TPSA 63.3 Open detail RCSB PDB

4MV PDB via homolog Detail RCSB PDB

AKG PDB via homolog Detail RCSB PDB

GBN PDB via homolog Detail RCSB PDB

GUA 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
2ML RCSB PDB	1I1L	P0AB80	145.2 Da LogP 0.83 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)C[C@@](C)(C(=O)O)N`
4MV RCSB PDB	1I1M	P0AB80	116.2 Da LogP 1.51 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC(=O)O`
AKG RCSB PDB	5E25	A0A0A7GJ30	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
GBN RCSB PDB	2EJ3	Q5SM19	171.2 Da LogP 1.37 TPSA 63.3	✓ Ro5	✓ Clean	`C1CCC(CC1)(CC(=O)O)CN`
GUA RCSB PDB	1IYD	P0AB80	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
PGU RCSB PDB	1IYE	P0AB80	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…`
PMP RCSB PDB	6Q8E	D1CCW1	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
PPE RCSB PDB	2EJ2	Q5SM19	379.3 Da LogP -0.47 TPSA 187.8	1 viol.	✓ Clean	`Cc1c(c(c(c[nH+]1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)…`
PXG RCSB PDB	5MR0	O29329	368.3 Da LogP 2.02 TPSA 149.2	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cccc(c2)C(=O)O)O`
PY5 RCSB PDB	6THQ	F2L0W0	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`
TAM RCSB PDB	5MQZ	O29329	163.2 Da LogP -1.17 TPSA 86.7	✓ Ro5	✓ Clean	`C(CO)C(CCO)(CCO)N`

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
ZINC1703342 ZINC	0.786	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
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`
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`
ZINC157284 ZINC	0.739	200.2 Da LogP 1.89 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CC1(CC(=O)O)CCCCC1`
ZINC395014 ZINC	0.739	214.3 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CC1(CC(=O)O)CCCCCC1`
ZINC3074815 ZINC	0.688	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCC(=O)O`
ZINC75149343 ZINC	0.679	221.3 Da LogP -0.39 TPSA 97.5	✓ Ro5	✓ Clean	`NCC1(CC(=O)O)CCS(=O)(=O)CC1`
ZINC2508031 ZINC	0.667	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC4828816 ZINC	0.647	217.2 Da LogP 1.33 TPSA 107.2	✓ Ro5	✓ Clean	`O=C(O)CCCC(CCCC(=O)O)=NO`
ZINC1841074 ZINC	0.636	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCC(=O)O`
ZINC2013445 ZINC	0.636	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCC(=O)O`
ZINC2575042 ZINC	0.636	228.4 Da LogP 4.63 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCC(=O)O`
ZINC2575038 ZINC	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC26897400 ZINC	0.625	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813 ZINC	0.625	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725 ZINC	0.625	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898 ZINC	0.625	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900 ZINC	0.625	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC231485617 ZINC	0.607	214.3 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCC1(CC(=O)O)CCCCC1`
ZINC49816868 ZINC	0.600	214.3 Da LogP 1.08 TPSA 92.4	✓ Ro5	✓ Clean	`NC(=O)NCC1(CC(=O)O)CCCCC1`
ZINC1532708 ZINC	0.596	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC13433578 ZINC	0.588	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC14510370 ZINC	0.588	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061 ZINC	0.588	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426 ZINC	0.588	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567 ZINC	0.588	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3861297 ZINC	0.588	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502 ZINC	0.588	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109 ZINC	0.588	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC145838685 ZINC	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@@H](C)CCCC(=O)O`
ZINC145838882 ZINC	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](C)CCCC(=O)O`
ZINC98175207 ZINC	0.579	290.3 Da LogP 0.58 TPSA 127.2	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)OCCOC(=O)CCCC(=O)O`
ZINC1532705 ZINC	0.577	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC35837411 ZINC	0.567	214.3 Da LogP 1.97 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)CC1(CC(=O)O)CCCCC1`
ZINC1857524090 ZINC	0.560	242.4 Da LogP 3.81 TPSA 54.4	✓ Ro5	✓ Clean	`CC(C)CCCC(=O)CCCCCCC(=O)O`
ZINC115371230 ZINC	0.556	266.4 Da LogP 2.88 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCSSCCCCC(=O)O`
ZINC12954423 ZINC	0.556	232.4 Da LogP 3.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCS`
ZINC13357569 ZINC	0.556	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC138216182 ZINC	0.556	293.2 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCBr`
ZINC1661158 ZINC	0.556	234.3 Da LogP 2.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCSCCCCC(=O)O`
ZINC1763117 ZINC	0.556	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1841307 ZINC	0.556	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCC(=O)O`
ZINC34552398 ZINC	0.556	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306 ZINC	0.556	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC5855130 ZINC	0.556	242.4 Da LogP 3.95 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCCC(=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.

Cross-references

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

Sequence

UniProt A0A0H3GPS2

Pathways

KEGG R01090 BioCyc BRANCHED-CHAINAMINOTRANSFERLEU-RXN KEGG R01214 BioCyc BRANCHED-CHAINAMINOTRANSFERVAL-RXN KEGG R02199 BioCyc BRANCHED-CHAINAMINOTRANSFERILEU-RXN