Protein profile

PA1629

enoyl-CoA hydratase

Genome: NC_002516.2

Gene: PA1629 Structure source: AlphaFold UniProt Q9I393
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Amino acids 261
Annotations 3
Features 13
PDB binders 7
Druggability 0.801

Overview

Basic information about this protein and its source genome.

Accession
PA1629
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1629
Status
annotated
Amino acids
261
Structure source
AlphaFold
GO
GO:0016836 Catalysis of the cleavage of a carbon-oxygen bond by elimination of water. GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
46.281
Human E-value
4.39e-70
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
Cytoplasmic

Selected Druggability evidence

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 0.801
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

3 GO

Gene Ontology (GO)

3
  • GO:0016836 Catalysis of the cleavage of a carbon-oxygen bond by elimination of water.
  • GO:0006635 A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

13 records
Show feature table
Start End DB Term Name
17 200 CDD cd06558 crotonase-like
11 255 PANTHER PTHR11941 ENOYL-COA HYDRATASE-RELATED
202 261 FunFam G3DSA:1.10.12.10:FF:000001 Probable enoyl-CoA hydratase, mitochondrial
7 260 SUPERFAMILY SSF52096 ClpP/crotonase
7 260 InterPro IPR029045 ClpP/crotonase-like domain superfamily
6 201 FunFam G3DSA:3.90.226.10:FF:000009 Carnitinyl-CoA dehydratase
102 122 ProSitePatterns PS00166 Enoyl-CoA hydratase/isomerase signature.
102 122 InterPro IPR018376 Enoyl-CoA hydratase/isomerase, conserved site
203 260 Gene3D G3DSA:1.10.12.10 -
203 260 InterPro IPR014748 Enoyl-CoA hydratase, C-terminal
6 202 Gene3D G3DSA:3.90.226.10 -
16 260 Pfam PF00378 Enoyl-CoA hydratase/isomerase
16 260 InterPro IPR001753 Enoyl-CoA hydratase/isomerase

3D Structure

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

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Structural evidence

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1629
AlphaFold — — full sequence — Viewing
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 0.801
3 0.745

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.

58 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
BEZ
3R9S
A0A0H2ZTH2 122.1 Da LogP 1.38 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)O
CAA
1DUB
P14604 851.6 Da LogP -1.36 TPSA 380.7 3 viol. ✓ Clean CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
CO8
2DUB
P14604 893.7 Da LogP 1.03 TPSA 363.6 3 viol. ✓ Clean CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
COO
2HW5
P30084 835.6 Da LogP -0.76 TPSA 363.6 3 viol. ✓ Clean CC=CC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C)CO[P@@](…
DAK
1EY3
P14604 940.8 Da LogP 0.44 TPSA 366.9 3 viol. Alert CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
HXC
1MJ3
P14604 865.7 Da LogP 0.25 TPSA 363.6 3 viol. ✓ Clean CCCCCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P@@…
MLI
5JBX
Q1D5Y4 102.0 Da LogP -3.12 TPSA 80.3 ✓ 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.