Protein profile

PA2189

hypothetical protein

Genome: NC_002516.2

Gene: PA2189 Structure source: AlphaFold UniProt Q9I1S6
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Amino acids 184
Annotations 5
Features 8
PDB binders 2
Druggability 0.571

Overview

Basic information about this protein and its source genome.

Accession
PA2189
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2189
Status
annotated
Amino acids
184
Structure source
AlphaFold
GO
GO:0009368 A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form. GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis. GO:0051117 Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP. GO:0004252 Catalysis of the hydrolysis of internal, alpha-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:0006515 The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

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 0.571
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:0009368 A protein complex comprised of members of the ClpX, ClpC, ClpD, ClpP or ClpR protein families. ClpPs are the proteolytic subunit of active complexes, and ClpA and ClpX form the regulatory subunits. Enzymatically active and inactive complexes can form.
  • GO:0004176 Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
  • GO:0051117 Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.
  • GO:0004252 Catalysis of the hydrolysis of internal, alpha-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:0006515 The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.

Sequence Features

Domain/signature hits from InterPro and related databases.

8 records
Show feature table
Start End DB Term Name
26 46 Coils Coil Coil
3 174 PANTHER PTHR10381 ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT
3 174 InterPro IPR023562 Clp protease proteolytic subunit /Translocation-enhancing protein TepA
1 173 Gene3D G3DSA:3.90.226.10 -
2 168 Pfam PF00574 Clp protease
2 168 InterPro IPR023562 Clp protease proteolytic subunit /Translocation-enhancing protein TepA
3 170 SUPERFAMILY SSF52096 ClpP/crotonase
3 170 InterPro IPR029045 ClpP/crotonase-like 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 PA2189
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 0.571

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.

52 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
39Y
4U0G
P9WPC5 142.2 Da LogP 2.06 TPSA 37.3 ✓ Ro5 ✓ Clean CC[C@H](C)C/C=C/C(=O)O
ZIL
4U0G
P9WPC5 378.5 Da LogP 2.94 TPSA 104.7 ✓ Ro5 ✓ Clean CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)O)NC(…

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.