Protein profile

PA4121

hypothetical protein

Genome: NC_002516.2

Gene: PA4121 Structure source: AlphaFold UniProt Q9HWR0
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Amino acids 219
Annotations 4
Features 10
PDB binders 3
Druggability 0.913

Overview

Basic information about this protein and its source genome.

Accession
PA4121
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4121
Status
annotated
Amino acids
219
Structure source
AlphaFold
GO
GO:0008704 Catalysis of the reaction: 5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate. GO:0018800 Catalysis of the reaction: 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2. GO:0046872 Binding to a metal ion. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.897
Human E-value
1.4999999999999998e-24
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 0.913
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:0008704 Catalysis of the reaction: 5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate.
  • GO:0018800 Catalysis of the reaction: 5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2.
  • GO:0046872 Binding to a metal ion.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records
Show feature table
Start End DB Term Name
5 219 Gene3D G3DSA:3.90.850.10 -
5 219 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily
6 218 PANTHER PTHR11820 ACYLPYRUVASE
14 216 Pfam PF01557 Fumarylacetoacetate (FAA) hydrolase family
14 216 InterPro IPR011234 Fumarylacetoacetase-like, C-terminal
11 217 SUPERFAMILY SSF56529 FAH
11 217 InterPro IPR036663 Fumarylacetoacetase-like, C-terminal domain superfamily
6 219 FunFam G3DSA:3.90.850.10:FF:000020 Putative 4-hydroxyphenylacetate degradation bifunctional isomerase
11 216 NCBIfam TIGR02305 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit
11 216 InterPro IPR012686 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase, N-terminal subunit

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

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 PA4121
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 0.913

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.

18 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
OXL
6FOG
Q6P587-1 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
PYR
6J5X
Q8NLC0 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)C(=O)O
TAR
3V77
D2YW46 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@H]([C@@H](C(=O)O)O)(C(=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.