Protein profile

PA4127

2-oxo-hepta-3-ene-1,7-dioic acid hydratase

Genome: NC_002516.2

Gene: hpcG PA4127 Structure source: AlphaFold UniProt Q9HWQ4
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Amino acids 267
Annotations 5
Features 11
PDB binders 3
Druggability 0.709

Overview

Basic information about this protein and its source genome.

Accession
PA4127
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
hpcG PA4127
Status
annotated
Amino acids
267
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0018817 Catalysis of the reaction: cis-2-oxohept-3-ene-1,7-dioate + H2O = 2,4-dihydroxy-hept-trans-2-ene-1,7-dioate. GO:0008684 Catalysis of the reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O. 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. GO:0019439 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
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 0.709
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MLDPRLIQEAANRLDAAERSRQQVRQFSLDYPDIAIEDAYAIQRAWVERKIADGRVLKGHKIGLTSRAMQVSSNISEPDYGALLDDMFFEEGSDIPFQRFIVPRVEVELAFILGKPLKGPGCTLFDVLEATEWVIPALEIIDARIQQVDPQTKVTRKVFDTISDNAANAGVVMGGRAVRPGDIDLRRVPAILYRNGVIEESGVSAAVLNHPAKGVAWLANKLAPYGVCLEAGQVILGGSFTRPVAAAPGDTFHVDYDLLGSISCRFV

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0018817 Catalysis of the reaction: cis-2-oxohept-3-ene-1,7-dioate + H2O = 2,4-dihydroxy-hept-trans-2-ene-1,7-dioate.
  • GO:0008684 Catalysis of the reaction: 4-hydroxy-2-oxopentanoate = 2-oxopent-4-enoate + H2O.
  • 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.
  • GO:0019439 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring.

Sequence Features

Domain/signature hits from InterPro and related databases.

11 records
Show feature table
Start End DB Term Name
5 267 PANTHER PTHR30143 ACID HYDRATASE
103 266 Pfam PF01557 Fumarylacetoacetate (FAA) hydrolase family
103 266 InterPro IPR011234 Fumarylacetoacetase-like, C-terminal
7 27 Coils Coil Coil
1 267 NCBIfam TIGR02312 2-oxo-hepta-3-ene-1,7-dioic acid hydratase
1 267 InterPro IPR012690 2-oxo-hepta-4-ene-1,7-dioic acid hydratase
1 267 FunFam G3DSA:3.90.850.10:FF:000001 2-oxo-hepta-3-ene-1,7-dioic acid hydratase
1 267 Gene3D G3DSA:3.90.850.10 -
1 267 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily
3 267 SUPERFAMILY SSF56529 FAH
3 267 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily

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 PA4127
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
2 0.709

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.

53 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
0L1
5D2J
Q1XGK3 146.1 Da LogP 0.72 TPSA 74.6 ✓ Ro5 ✓ Clean C(CCC(=O)O)CC(=O)O
AKG
5D2H
Q1XGK3 146.1 Da LogP -0.50 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)O)C(=O)C(=O)O
OOG
5D2K
Q1XGK3 160.1 Da LogP -0.11 TPSA 91.7 ✓ Ro5 ✓ Clean C(CC(=O)C(=O)O)CC(=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.