Protein profile

PA1610

3-hydroxydecanoyl-ACP dehydratase

Genome: NC_002516.2

Gene: PA1610 fabA Structure source: Experimental + AlphaFold UniProt O33877
Export view
Amino acids 171
Annotations 9
Features 14
PDB binders 13
Druggability 0.833

Overview

Basic information about this protein and its source genome.

Accession
PA1610
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1610 fabA
Status
annotated
Amino acids
171
Structure source
Experimental + AlphaFold
EC
4.2.1.59 5.3.3.14
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0019171 Catalysis of the reaction: a (3R)-hydroxyacyl-[acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O. GO:0034017 Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein]. 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:0006636 The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

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 0.833
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 7 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

7
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0019171 Catalysis of the reaction: a (3R)-hydroxyacyl-[acyl-carrier-protein] = a (2E)-enoyl-[acyl-carrier-protein] + H2O.
  • GO:0034017 Catalysis of the reaction: trans-dec-2-enoyl-[acyl-carrier protein] = cis-dec-3-enoyl-[acyl-carrier protein].
  • 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:0006636 The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0008693 OBSOLETE. Catalysis of the reaction: (3R)-3-hydroxydecanoyl-[acyl-carrier protein] = 2,3-decenoyl-[acyl-carrier protein] or 3,4-decenoyl-[acyl-carrier protein] + H2O.

Sequence Features

Domain/signature hits from InterPro and related databases.

14 records
Show feature table
Start End DB Term Name
3 171 NCBIfam TIGR01749 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA
3 171 InterPro IPR010083 Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
26 165 CDD cd01287 FabA
26 165 InterPro IPR010083 Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
1 171 Hamap MF_00405 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase [fabA].
1 171 InterPro IPR010083 Beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabA
2 168 SUPERFAMILY SSF54637 Thioesterase/thiol ester dehydrase-isomerase
2 168 InterPro IPR029069 HotDog domain superfamily
1 171 Gene3D G3DSA:3.10.129.10 Hotdog Thioesterase
28 157 Pfam PF07977 FabA-like domain
28 157 InterPro IPR013114 Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ
28 159 PANTHER PTHR30272 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE
28 159 InterPro IPR013114 Beta-hydroxydecanoyl thiol ester dehydrase, FabA/FabZ
1 171 FunFam G3DSA:3.10.129.10:FF:000003 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase

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

Loading 3D structure...

Legend High Medium Low

Structural evidence

12 + 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 8B72
X-ray 1.87 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Viewing
PDB 7BKA
X-ray 1.88 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4B0B
X-ray 1.90 Å A,B
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 7BK9
X-ray 1.94 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 7BIS
X-ray 1.96 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4FQ9
X-ray 2.02 Å A,B,C,D,E,F,G,H,I,J
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4B0I
X-ray 2.03 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 7BHJ
X-ray 2.11 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4CL6
X-ray 2.41 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4B0J
X-ray 2.50 Å A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4B0C
X-ray 2.70 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
PDB 4B8U
X-ray 2.76 Å A,B,C,D,E
100.0% 1-171
PDBe RCSB PDBj File
Loaded
AlphaFold PA1610
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 0.833
2 0.339

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 2.61 0.076
2 1.05 0.006

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.

63 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
3MQ
4B0J 2.50 Å Open crystal
181.2 Da LogP 1.90 TPSA 46.3 ✓ Ro5 ✓ Clean c1cc(sc1)c2cc(no2)CO
4JC
7BKA 1.88 Å Open crystal
185.2 Da LogP 0.90 TPSA 60.2 ✓ Ro5 ✓ Clean CCc1ccc(cc1)S(=O)(=O)N
54F
4B0B 1.90 Å Open crystal
186.2 Da LogP 2.46 TPSA 48.1 ✓ Ro5 ✓ Clean c1ccnc(c1)Oc2cccc(c2)N
7SB
4CL6 2.41 Å Open crystal
274.7 Da LogP 3.33 TPSA 66.7 ✓ Ro5 ✓ Clean c1cc(oc1)c2[nH]nc(n2)NCc3ccc(cc3)Cl
C9H
4B0C 2.70 Å Open crystal
171.3 Da LogP 2.09 TPSA 41.6 ✓ Ro5 ✓ Clean CCCCCSc1[nH]ncn1
IBK
4B8U 2.76 Å Open crystal
294.4 Da LogP 2.69 TPSA 64.4 ✓ Ro5 ✓ Clean CC(C)CNC(=O)COCc1cc(on1)c2cccs2
KBP
4B0I 2.03 Å Open crystal
289.4 Da LogP 2.49 TPSA 66.4 ✓ Ro5 ✓ Clean CCCCCCC[C@H](CC(=O)SCCNC(=O)C)O
TQH
7BHJ 2.11 Å Open crystal
260.3 Da LogP 3.05 TPSA 66.7 ✓ Ro5 ✓ Clean Cc1ccc(o1)CNc2[nH]c(nn2)c3cccs3
TZQ
7BIS 1.96 Å Open crystal
270.6 Da LogP 3.35 TPSA 59.7 ✓ Ro5 ✓ Clean c1cc(c(cc1OCc2ccc(o2)C(=O)O)Cl)F
U0W
7BK9 1.94 Å Open crystal
258.3 Da LogP 3.05 TPSA 59.7 ✓ Ro5 ✓ Clean c1cc2c(cc1OCc3ccc(o3)C(=O)O)CCC2

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.