Protein profile

PA1806

NADH-dependent enoyl-ACP reductase

Genome: NC_002516.2

Gene: PA1806 fabI Structure source: Experimental + AlphaFold UniProt Q9ZFE4
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Amino acids 265
Annotations 5
Features 24
PDB binders 17
Druggability 0.84

Overview

Basic information about this protein and its source genome.

Accession
PA1806
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1806 fabI
Status
annotated
Amino acids
265
Structure source
Experimental + AlphaFold
EC
1.3.1.9
GO
GO:0004318 Catalysis of the reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + H+ + NADH. GO:0042802 Binding to an identical protein or proteins. GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.021
Human E-value
1.15e-07
Gut microbiome off-target
hit
Essential (DEG)
Y
Localization
CytoplasmicMembrane

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 0.84
Structure –
Pocket –

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:0004318 Catalysis of the reaction: a 2,3-saturated acyl-[ACP] + NAD+ = a (2E)-enoyl-[ACP] + H+ + NADH.
  • GO:0042802 Binding to an identical protein or proteins.
  • GO:0030497 The elongation of a fatty acid chain by the sequential addition of two-carbon units.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
6 255 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
6 255 InterPro IPR036291 NAD(P)-binding domain superfamily
13 255 Pfam PF13561 Enoyl-(Acyl carrier protein) reductase
85 96 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
85 96 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
183 200 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
183 200 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
218 238 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
218 238 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
136 152 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
136 152 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
162 181 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
162 181 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
8 25 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
8 25 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
1 265 Gene3D G3DSA:3.40.50.720 -
4 260 PANTHER PTHR43159 ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE
4 260 InterPro IPR014358 Enoyl-[acyl-carrier-protein] reductase (NADH)
6 260 CDD cd05372 ENR_SDR
6 260 InterPro IPR014358 Enoyl-[acyl-carrier-protein] reductase (NADH)
1 27 SignalP_GRAM_POSITIVE SignalP-TM SignalP-TM
1 263 PIRSF PIRSF000094 Enoyl-ACP_rdct
1 263 InterPro IPR014358 Enoyl-[acyl-carrier-protein] reductase (NADH)
1 265 FunFam G3DSA:3.40.50.720:FF:000054 Enoyl-[acyl-carrier-protein] reductase [NADH]

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

2 + 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 4NR0
X-ray 1.80 Å A,B,C,D
100.0% 1-265
PDBe RCSB PDBj File
Viewing
PDB 4NQZ
X-ray 2.60 Å A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P
100.0% 1-265
PDBe RCSB PDBj File
Loaded
AlphaFold PA1806
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 0.84

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 31.15 0.937
2 7.79 0.413

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.

127 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.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
TCL
4NR0 1.80 Å Open crystal
289.5 Da LogP 5.14 TPSA 29.5 1 viol. ✓ Clean c1cc(c(cc1Cl)O)Oc2ccc(cc2Cl)Cl

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.