Protein profile

PA1023

short-chain dehydrogenase

Genome: NC_002516.2

Gene: PA1023 Structure source: AlphaFold UniProt Q9I4V1
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Amino acids 305
Annotations 4
Features 22
PDB binders 3
Druggability 0.529

Overview

Basic information about this protein and its source genome.

Accession
PA1023
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1023
Status
annotated
Amino acids
305
Structure source
AlphaFold
GO
GO:0003857 Catalysis of the reaction: a (3S)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + NADH + H+. GO:0004300 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a enoyl-CoA + H2O. This reaction usually occurs in the reverse direction, leading to the reduction of the double bound of enoyl-CoA in position 2 or 3. Specific reactions catalyzed include: a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O and a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O. 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: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
hit
Human identity (%)
49.697
Human E-value
2.1e-46
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 0.529
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0003857 Catalysis of the reaction: a (3S)-3-hydroxyacyl-CoA + NAD+ = a 3-oxoacyl-CoA + NADH + H+.
  • GO:0004300 Catalysis of the reaction: a 3-hydroxy-fatty acyl-CoA = a enoyl-CoA + H2O. This reaction usually occurs in the reverse direction, leading to the reduction of the double bound of enoyl-CoA in position 2 or 3. Specific reactions catalyzed include: a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O and a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O.
  • 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: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.

22 records
Show feature table
Start End DB Term Name
1 283 PANTHER PTHR45024 DEHYDROGENASES, SHORT CHAIN
7 253 SUPERFAMILY SSF51735 NAD(P)-binding Rossmann-fold domains
7 253 InterPro IPR036291 NAD(P)-binding domain superfamily
166 185 PRINTS PR00080 Short-chain dehydrogenase/reductase (SDR) superfamily signature
166 185 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
146 154 PRINTS PR00080 Short-chain dehydrogenase/reductase (SDR) superfamily signature
146 154 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
93 104 PRINTS PR00080 Short-chain dehydrogenase/reductase (SDR) superfamily signature
93 104 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
153 181 ProSitePatterns PS00061 Short-chain dehydrogenases/reductases family signature.
153 181 InterPro IPR020904 Short-chain dehydrogenase/reductase, conserved site
15 249 Pfam PF13561 Enoyl-(Acyl carrier protein) reductase
9 253 Gene3D G3DSA:3.40.50.720 -
140 156 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
140 156 InterPro IPR002347 Short-chain dehydrogenase/reductase SDR
10 27 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
10 27 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
93 104 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
166 185 PRINTS PR00081 Glucose/ribitol dehydrogenase family signature
9 205 SMART SM00822 This enzymatic domain is part of bacterial polyketide synthases and catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.

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 PA1023
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 0.529
3 0.215

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
1PS
4URE
Q5P8S7 201.2 Da LogP -0.09 TPSA 61.1 ✓ Ro5 ✓ Clean c1cc[n+](cc1)CCCS(=O)(=O)[O-]
3HL
2ZTL
Q5KST5 104.1 Da LogP -0.16 TPSA 57.5 ✓ Ro5 ✓ Clean C[C@@H](CC(=O)O)O
RM4
7DO7
C1DMX5 164.2 Da LogP -2.19 TPSA 90.2 ✓ Ro5 ✓ Clean C[C@H]1[C@@H]([C@H]([C@H]([C@H](O1)O)O)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.