Protein profile

PA3426

enoyl-CoA hydratase

Genome: NC_002516.2

Gene: PA3426 Structure source: AlphaFold UniProt Q9HYH9
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Amino acids 256
Annotations 1
Features 10
PDB binders 9
Druggability 0.865

Overview

Basic information about this protein and its source genome.

Accession
PA3426
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3426
Status
annotated
Amino acids
256
Structure source
AlphaFold
GO
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 (%)
33.88
Human E-value
3.04e-14
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 0.865
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

1
  • 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.

10 records
Show feature table
Start End DB Term Name
3 252 SUPERFAMILY SSF52096 ClpP/crotonase
3 252 InterPro IPR029045 ClpP/crotonase-like domain superfamily
1 198 Gene3D G3DSA:3.90.226.10 -
97 117 ProSitePatterns PS00166 Enoyl-CoA hydratase/isomerase signature.
97 117 InterPro IPR018376 Enoyl-CoA hydratase/isomerase, conserved site
3 255 PANTHER PTHR43802 ENOYL-COA HYDRATASE
8 246 Pfam PF00378 Enoyl-CoA hydratase/isomerase
8 246 InterPro IPR001753 Enoyl-CoA hydratase/isomerase
199 256 Gene3D G3DSA:1.10.287.2460 -
3 185 CDD cd06558 crotonase-like

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 + 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 PA3426
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
1 0.865
2 0.543

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.

59 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
5F9
5DTW
P9WNP1 1062.1 Da LogP 5.71 TPSA 363.6 4 viol. ✓ Clean CCCCCCCCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](…
5FF
5DU4
P9WNP1 458.5 Da LogP 5.04 TPSA 68.2 1 viol. ✓ Clean CCc1ccc(cc1)[C@H]2C[C@H](n3c(c(cn3)C(=O)NCc4ccc…
5FK
5DU8
P9WNP1 447.4 Da LogP 4.57 TPSA 71.8 ✓ Ro5 ✓ Clean CCc1ccc(cc1)[C@H]2C[C@H](n3c(c(cn3)C(=O)NCc4ccc…
BCA
1JXZ
A5JTM5 887.6 Da LogP -0.32 TPSA 383.9 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H](…
BEZ
3R9S
A0A0H2ZTH2 122.1 Da LogP 1.38 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)O
G51
5DUC
P9WNP1 472.5 Da LogP 4.76 TPSA 77.4 ✓ Ro5 ✓ Clean CCc1ccc(cc1)[C@H]2C[C@H](n3c(c(cn3)C(=O)NCc4ccc…
G59
5DU6
P9WNP1 392.5 Da LogP 4.63 TPSA 59.0 ✓ Ro5 ✓ Clean CCc1ccc(cc1)[C@H]2C[C@H](n3c(c(cn3)C(=O)NCc4ccc…
G7A
5DUF
P9WNP1 339.3 Da LogP 3.80 TPSA 67.2 ✓ Ro5 ✓ Clean CCc1ccc(cc1)[C@H]2C[C@H](n3c(c(cn3)C(=O)O)N2)C(…
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.