Protein profile

KP13_03660

Acyl-CoA thioesterase 2

Genome: KpKP13

Gene: tesB AHE46002.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GJ69
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Amino acids 287
Annotations 5
Features 14
PDB binders 2
Druggability 0.359

Overview

Basic information about this protein and its source genome.

Accession
KP13_03660
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
tesB AHE46002.1
Status
annotated
Amino acids
287
Structure source
AlphaFold + ColabFold
EC
3.1.2.20
GO
GO:0006637 The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group. GO:0047617 Catalysis of the reaction: a fatty acyl-CoA + H2O = a fatty acid + CoA + H+. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0009062 The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
50.0
Human E-value
1.3e-07
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.37

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 0.359
Structure A0A0H3GJ69
Pocket Pocket 2
P2Rank 0.939
Structure A0A0H3GJ69
Pocket Pocket 1
ColabFold model
FPocket 0.962 · Pocket 17
P2Rank 0.942 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 155 / 4744 genomes with a hit
Normalized 0.033

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0006637 The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group.
  • GO:0047617 Catalysis of the reaction: a fatty acyl-CoA + H2O = a fatty acid + CoA + H+.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0009062 The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
21 109 CDD cd03445 Thioesterase_II_repeat2
12 283 NCBIfam TIGR00189 acyl-CoA thioesterase II
12 283 InterPro IPR003703 Acyl-CoA thioesterase
33 282 Pfam PF13622 Thioesterase-like superfamily
5 114 SUPERFAMILY SSF54637 Thioesterase/thiol ester dehydrase-isomerase
5 114 InterPro IPR029069 HotDog domain superfamily
116 284 SUPERFAMILY SSF54637 Thioesterase/thiol ester dehydrase-isomerase
116 284 InterPro IPR029069 HotDog domain superfamily
1 286 Gene3D G3DSA:2.40.160.210 -
1 286 InterPro IPR042171 Acyl-CoA thioesterase, double hotdog domain
1 286 FunFam G3DSA:2.40.160.210:FF:000001 Acyl-CoA thioesterase II
5 285 PANTHER PTHR11066 ACYL-COA THIOESTERASE
5 285 InterPro IPR003703 Acyl-CoA thioesterase
178 282 CDD cd03444 Thioesterase_II_repeat1

3D Structure

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

3D visualization script Full viewer

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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_A0A0H3GJ69
AlphaFold — — full sequence — Viewing
ColabFold KP13_03660
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
2 0.359

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 Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 28.24 0.924

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.

16 records

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
LDA
1C8U
P0AGG2 229.4 Da LogP 4.48 TPSA 23.1 ✓ Ro5 ✓ Clean CCCCCCCCCCCC[N+](C)(C)[O-]
MLA
4R4U
Q8D151 104.1 Da LogP -0.45 TPSA 74.6 ✓ Ro5 ✓ Clean C(C(=O)O)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.