Protein profile

PA2950

reductase

Genome: NC_002516.2

Gene: PA2950 fabV Structure source: Experimental + AlphaFold UniProt Q9HZP8
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Amino acids 398
Annotations 7
Features 12
PDB binders 2
Druggability 0.849

Overview

Basic information about this protein and its source genome.

Accession
PA2950
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2950 fabV
Status
annotated
Amino acids
398
Structure source
Experimental + AlphaFold
EC
1.3.1.9 1.3.1.44
GO
GO:0004318 Catalysis of the reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + H+ + NADH. GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. GO:0050343 Catalysis of the reaction: acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH. GO:0006633 The chemical reactions and pathways resulting in the formation 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. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.849
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 5 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

5
  • GO:0004318 Catalysis of the reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + H+ + NADH.
  • GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
  • GO:0050343 Catalysis of the reaction: acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH.
  • GO:0006633 The chemical reactions and pathways resulting in the formation 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.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
1 392 Hamap MF_01838 Trans-2-enoyl-CoA reductase [NADH] [fabV].
1 392 InterPro IPR010758 Trans-2-enoyl-CoA reductase
1 397 FunFam G3DSA:3.40.50.720:FF:000221 Enoyl-[acyl-carrier-protein] reductase [NADH]
2 80 Pfam PF12242 NAD(P)H binding domain of trans-2-enoyl-CoA reductase
2 80 InterPro IPR010758 Trans-2-enoyl-CoA reductase
1 397 PANTHER PTHR37480 ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH]
1 397 InterPro IPR010758 Trans-2-enoyl-CoA reductase
323 386 Pfam PF07055 Enoyl reductase FAD binding domain
323 386 InterPro IPR024906 Enoyl reductase FAD binding domain
82 317 Pfam PF12241 Trans-2-enoyl-CoA reductase catalytic region
82 317 InterPro IPR024910 Trans-2-enoyl-CoA reductase catalytic domain, putative
1 398 Gene3D G3DSA:3.40.50.720 -

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

1 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 8RCZ
X-ray 2.25 Å A,B
100.0% 1-398
PDBe RCSB PDBj File
Viewing
AlphaFold PA2950
AlphaFold — — 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
1 0.849
4 0.251

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 17.09 0.795
2 10.44 0.561
3 3.91 0.154
4 2.44 0.066

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.

5 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
AEW
3ZU5
Q8Z9U1 298.4 Da LogP 3.91 TPSA 48.0 ✓ Ro5 ✓ Clean CCCCCCC1=CC(=O)N(C=C1)Cc2cccc(c2C)N
ZU4
3ZU4
Q8Z9U1 303.8 Da LogP 4.67 TPSA 22.0 ✓ Ro5 ✓ Clean CCCCCCC1=CC(=O)N(C=C1)Cc2ccccc2Cl

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.