Protein profile

PA4498

metallopeptidase

Genome: NC_002516.2

Gene: PA4498 Structure source: AlphaFold UniProt Q9HVS3
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Amino acids 405
Annotations 5
Features 15
PDB binders 3
Druggability 0.823

Overview

Basic information about this protein and its source genome.

Accession
PA4498
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4498
Status
annotated
Amino acids
405
Structure source
AlphaFold
GO
GO:0016805 Catalysis of the hydrolysis of a dipeptide. GO:0046872 Binding to a metal ion. GO:0070006 Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. GO:0042938 The directed movement of a dipeptide, a combination of two amino acids by means of a peptide (-CO-NH-) link, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
39.286
Human E-value
1.63e-12
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 0.823
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Gene Ontology (GO)

5
  • GO:0016805 Catalysis of the hydrolysis of a dipeptide.
  • GO:0046872 Binding to a metal ion.
  • GO:0070006 Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
  • GO:0042938 The directed movement of a dipeptide, a combination of two amino acids by means of a peptide (-CO-NH-) link, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records
Show feature table
Start End DB Term Name
169 402 Gene3D G3DSA:3.90.230.10 Creatinase/methionine aminopeptidase superfamily
169 402 InterPro IPR036005 Creatinase/aminopeptidase-like
15 169 SUPERFAMILY SSF53092 Creatinase/prolidase N-terminal domain
15 169 InterPro IPR029149 Creatinase/Aminopeptidase P/Spt16, N-terminal
29 395 PANTHER PTHR46112 AMINOPEPTIDASE
136 393 SUPERFAMILY SSF55920 Creatinase/aminopeptidase
136 393 InterPro IPR036005 Creatinase/aminopeptidase-like
35 169 Pfam PF01321 Creatinase/Prolidase N-terminal domain
35 169 InterPro IPR000587 Creatinase, N-terminal
1 168 Gene3D G3DSA:3.40.350.10 -
1 168 InterPro IPR029149 Creatinase/Aminopeptidase P/Spt16, N-terminal
178 384 Pfam PF00557 Metallopeptidase family M24
178 384 InterPro IPR000994 Peptidase M24
330 342 ProSitePatterns PS00491 Aminopeptidase P and proline dipeptidase signature.
330 342 InterPro IPR001131 Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site

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 PA4498
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 0.823

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
01B
5X49
Q9NQH7 195.2 Da LogP 0.00 TPSA 83.5 ✓ Ro5 ✓ Clean c1ccc(cc1)C[C@H]([C@@H](C(=O)O)O)N
12P
5X49
Q9NQH7 546.7 Da LogP -0.85 TPSA 142.0 2 viol. ✓ Clean C(COCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO)O
CAC
4ZNG
A8WBX8 137.0 Da LogP -0.52 TPSA 40.1 ✓ Ro5 ✓ Clean C[As](=O)(C)[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.