Protein profile

KP13_02696

Branched-chain-amino-acid aminotransferase

Genome: KpKP13

Gene: ilvE AHE47016.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GPS2

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Amino acids 309

Annotations 12

Features 17

PDB binders 11

Druggability 0.683

Overview

Basic information about this protein and its source genome.

Accession: KP13_02696
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: ilvE AHE47016.1
Status: annotated
Amino acids: 309
Structure source: AlphaFold + ColabFold

2.6.1.42

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.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 28.571
Human E-value: 5.99e-20
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 44.518
DEG E-value: 3.34e-87
Localization: Cytoplasmic
ColabFold pLDDT: 95.83

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.683

Structure A0A0H3GPS2

Pocket Pocket 4

P2Rank 0.916

Structure A0A0H3GPS2

Pocket Pocket 1

ColabFold model

FPocket 0.657 · Pocket 4

P2Rank 0.876 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 210 / 4744 genomes with a hit

Normalized 0.044

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 11 GO

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 Features

Domain/signature hits from InterPro and related databases.

17 records

Show feature table

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

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GPS2	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_02696	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
4				0.683
1				0.589

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	15.78	0.762
2	9.18	0.492
3	4.12	0.166
4	1.65	0.027
5	1.22	0.011

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
4				0.657

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	15.44	0.753
2	5.93	0.291
3	3.41	0.122
4	1.87	0.037
5	1.0	0.006

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	1I1L	P0AB80	145.2 Da LogP 0.83 TPSA 63.3	✓ Ro5	✓ Clean	`CC(C)C[C@@](C)(C(=O)O)N`
4MV	1I1M	P0AB80	116.2 Da LogP 1.51 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC(=O)O`
AKG	5E25	A0A0A7GJ30	146.1 Da LogP -0.50 TPSA 91.7	✓ Ro5	✓ Clean	`C(CC(=O)O)C(=O)C(=O)O`
GBN	2EJ3	Q5SM19	171.2 Da LogP 1.37 TPSA 63.3	✓ Ro5	✓ Clean	`C1CCC(CC1)(CC(=O)O)CN`
GUA	1IYD	P0AB80	132.1 Da LogP 0.33 TPSA 74.6	✓ Ro5	✓ Clean	`C(CC(=O)O)CC(=O)O`
PGU	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	6Q8E	D1CCW1	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1c(c(c(cn1)COP(=O)(O)O)CN)O`
PPE	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	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	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	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	0.786	202.2 Da LogP 1.07 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)CCCC(=O)O`
ZINC1529497	0.769	230.3 Da LogP 3.06 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCC(=O)O`
ZINC1531045	0.769	202.2 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)O`
ZINC1593115	0.769	216.3 Da LogP 2.67 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCC(=O)O`
ZINC1700020	0.769	244.3 Da LogP 3.45 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCC(=O)O`
ZINC3860440	0.769	258.4 Da LogP 3.84 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCC(=O)O`
ZINC3861298	0.769	286.4 Da LogP 4.62 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCC(=O)O`
ZINC5113062	0.769	272.4 Da LogP 4.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCC(=O)O`
ZINC157284	0.739	200.2 Da LogP 1.89 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CC1(CC(=O)O)CCCCC1`
ZINC395014	0.739	214.3 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CC1(CC(=O)O)CCCCCC1`
ZINC3074815	0.688	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCC(=O)O`
ZINC75149343	0.679	221.3 Da LogP -0.39 TPSA 97.5	✓ Ro5	✓ Clean	`NCC1(CC(=O)O)CCS(=O)(=O)CC1`
ZINC2508031	0.667	230.3 Da LogP 1.85 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCC(=O)CCCCC(=O)O`
ZINC4828816	0.647	217.2 Da LogP 1.33 TPSA 107.2	✓ Ro5	✓ Clean	`O=C(O)CCCC(CCCC(=O)O)=NO`
ZINC1841074	0.636	200.3 Da LogP 3.85 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCC(=O)O`
ZINC2013445	0.636	214.3 Da LogP 4.24 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCC(=O)O`
ZINC2575042	0.636	228.4 Da LogP 4.63 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCCCCCCCCCC(=O)O`
ZINC2575038	0.625	205.3 Da LogP 0.00 TPSA 86.7	✓ Ro5	✓ Clean	`NC(CCCO)(CCCO)CCCO`
ZINC26897400	0.625	286.4 Da LogP 3.41 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCCC(=O)O`
ZINC3074813	0.625	258.3 Da LogP 2.63 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCC(=O)CCCCCC(=O)O`
ZINC34423725	0.625	342.5 Da LogP 4.97 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCCCCC(=O)O`
ZINC4822898	0.625	272.3 Da LogP 3.02 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCC(=O)CCCCCC(=O)O`
ZINC4822900	0.625	300.4 Da LogP 3.80 TPSA 91.7	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCC(=O)CCCCCC(=O)O`
ZINC231485617	0.607	214.3 Da LogP 2.28 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCC1(CC(=O)O)CCCCC1`
ZINC49816868	0.600	214.3 Da LogP 1.08 TPSA 92.4	✓ Ro5	✓ Clean	`NC(=O)NCC1(CC(=O)O)CCCCC1`
ZINC1532708	0.596	248.2 Da LogP 0.16 TPSA 125.9	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CN)c1O`
ZINC13433578	0.588	201.3 Da LogP 1.68 TPSA 80.4	✓ Ro5	✓ Clean	`NC(=O)CCCCCCCCC(=O)O`
ZINC14510370	0.588	244.4 Da LogP 3.74 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCO`
ZINC1531061	0.588	216.3 Da LogP 2.96 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCO`
ZINC1610426	0.588	230.3 Da LogP 3.35 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCO`
ZINC2168567	0.588	202.3 Da LogP 2.57 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCO`
ZINC3861297	0.588	272.4 Da LogP 4.52 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCO`
ZINC4284502	0.588	258.4 Da LogP 4.13 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCO`
ZINC5287109	0.588	286.5 Da LogP 4.91 TPSA 57.5	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCCCCCO`
ZINC145838685	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@@H](C)CCCC(=O)O`
ZINC145838882	0.583	200.3 Da LogP 3.70 TPSA 37.3	✓ Ro5	✓ Clean	`CC(C)CCC[C@H](C)CCCC(=O)O`
ZINC98175207	0.579	290.3 Da LogP 0.58 TPSA 127.2	✓ Ro5	✓ Clean	`O=C(O)CCCC(=O)OCCOC(=O)CCCC(=O)O`
ZINC1532705	0.577	249.2 Da LogP 0.20 TPSA 120.1	✓ Ro5	✓ Clean	`Cc1ncc(COP(=O)(O)O)c(CO)c1O`
ZINC35837411	0.567	214.3 Da LogP 1.97 TPSA 63.6	✓ Ro5	✓ Clean	`COC(=O)CC1(CC(=O)O)CCCCC1`
ZINC1857524090	0.560	242.4 Da LogP 3.81 TPSA 54.4	✓ Ro5	✓ Clean	`CC(C)CCCC(=O)CCCCCCC(=O)O`
ZINC115371230	0.556	266.4 Da LogP 2.88 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCSSCCCCC(=O)O`
ZINC12954423	0.556	232.4 Da LogP 3.90 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCS`
ZINC13357569	0.556	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCC(=O)O`
ZINC138216182	0.556	293.2 Da LogP 4.76 TPSA 37.3	✓ Ro5	✓ Clean	`O=C(O)CCCCCCCCCCCCBr`
ZINC1661158	0.556	234.3 Da LogP 2.23 TPSA 74.6	✓ Ro5	✓ Clean	`O=C(O)CCCCSCCCCC(=O)O`
ZINC1763117	0.556	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCC(=O)O`
ZINC1841307	0.556	228.3 Da LogP 3.56 TPSA 54.4	✓ Ro5	✓ Clean	`CC(=O)CCCCCCCCCCC(=O)O`
ZINC34552398	0.556	257.4 Da LogP 4.10 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCC(=O)O`
ZINC34628306	0.556	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`NCCCCCCCCCCCCCCCC(=O)O`
ZINC5855130	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.