Protein profile

PA1327

protease

Genome: NC_002516.2

Gene: PA1327 Structure source: AlphaFold UniProt Q9I417
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Amino acids 656
Annotations 7
Features 27
PDB binders 0
Druggability 0.47

Overview

Basic information about this protein and its source genome.

Accession
PA1327
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1327
Status
annotated
Amino acids
656
Structure source
AlphaFold
EC
3.4.21.-
GO
GO:0004519 Catalysis of the cleavage of ester linkages within nucleic acids by creating internal breaks. GO:0046872 Binding to a metal ion. GO:0003676 Binding to a nucleic acid. GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
27.957
Human E-value
3.57e-10
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Extracellular

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 0.47
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0004519 Catalysis of the cleavage of ester linkages within nucleic acids by creating internal breaks.
  • GO:0046872 Binding to a metal ion.
  • GO:0003676 Binding to a nucleic acid.
  • GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
28 608 PANTHER PTHR13966 ENDONUCLEASE RELATED
28 608 InterPro IPR040255 Non-specific endonuclease
390 603 Pfam PF01223 DNA/RNA non-specific endonuclease
390 603 InterPro IPR001604 DNA/RNA non-specific endonuclease
379 610 FunFam G3DSA:3.40.570.10:FF:000013 Serine protease
391 605 CDD cd00091 NUC
379 607 Gene3D G3DSA:3.40.570.10 Extracellular Endonuclease, subunit A
379 607 InterPro IPR044929 DNA/RNA non-specific endonuclease superfamily
300 312 PRINTS PR00839 V8 serine protease family signature
300 312 InterPro IPR008256 Peptidase S1B
134 151 PRINTS PR00839 V8 serine protease family signature
134 151 InterPro IPR008256 Peptidase S1B
282 298 PRINTS PR00839 V8 serine protease family signature
282 298 InterPro IPR008256 Peptidase S1B
134 308 Pfam PF13365 Trypsin-like peptidase domain
386 601 SUPERFAMILY SSF54060 His-Me finger endonucleases
386 601 InterPro IPR044925 His-Me finger superfamily
107 330 SUPERFAMILY SSF50494 Trypsin-like serine proteases
107 330 InterPro IPR009003 Peptidase S1, PA clan
397 604 SMART SM00477 endoplus
397 604 InterPro IPR020821 Extracellular Endonuclease, subunit A
113 224 Gene3D G3DSA:2.40.10.10 -
113 224 InterPro IPR043504 Peptidase S1, PA clan, chymotrypsin-like fold
396 604 SMART SM00892 Endonuclease_NS_2
396 604 InterPro IPR001604 DNA/RNA non-specific endonuclease
225 322 Gene3D G3DSA:2.40.10.10 -
225 322 InterPro IPR043504 Peptidase S1, PA clan, chymotrypsin-like fold

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 PA1327
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 0.47
1 0.338

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.

3 records

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

Show only:
Ligand UniProt (homolog) pchembl MW · LogP · TPSA Lipinski PAINS SMILES
CHEMBL3327268 Q14249 — 515.6 Da LogP 5.37 TPSA 82.4 2 viol. Alert CC(=O)Oc1cccc(N2C(=O)/C(=C/N3N=C(c4ccccc4)CC3c3…

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.