Overview
Basic information about this protein and its source genome.
- Accession
- PA5053
- Gene
- hslV PA5053
- Status
- annotated
- Amino acids
- 177
- Structure source
- AlphaFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Enzyme Commission (EC)
1Gene Ontology (GO)
7- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0009376 A protein complex that possesses ATP-dependent protease activity; consists of an ATPase large subunit with homology to other ClpX family ATPases and a peptidase small subunit related to the proteasomal beta-subunits of eukaryotes. In the E. coli complex, a double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer.
- GO:0005839 A multisubunit barrel shaped endoprotease complex, which is the core of the proteasome complex.
- GO:0046872 Binding to a metal ion.
- GO:0004298 Catalysis of the hydrolysis of internal peptide bonds in a polypeptide chain by a mechanism in which the hydroxyl group of a threonine residue at the active center acts as a nucleophile.
- GO:0051603 OBSOLETE. The hydrolysis of a peptide bond or bonds within a protein as part of the chemical reactions and pathways resulting in the breakdown of a protein by individual cells.
- 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.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 174 | Gene3D | G3DSA:3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| 1 | 174 | InterPro | IPR029055 | Nucleophile aminohydrolases, N-terminal |
| 1 | 173 | Hamap | MF_00248 | ATP-dependent protease subunit HslV [hslV]. |
| 1 | 173 | InterPro | IPR022281 | ATP-dependent protease, HslV subunit |
| 2 | 171 | Pfam | PF00227 | Proteasome subunit |
| 2 | 171 | InterPro | IPR001353 | Proteasome, subunit alpha/beta |
| 2 | 173 | NCBIfam | TIGR03692 | HslU--HslV peptidase proteolytic subunit |
| 2 | 173 | InterPro | IPR022281 | ATP-dependent protease, HslV subunit |
| 1 | 176 | PIRSF | PIRSF039093 | HslV |
| 1 | 176 | InterPro | IPR022281 | ATP-dependent protease, HslV subunit |
| 1 | 174 | FunFam | G3DSA:3.60.20.10:FF:000002 | ATP-dependent protease subunit HslV |
| 2 | 174 | PANTHER | PTHR32194 | METALLOPROTEASE TLDD |
| 2 | 174 | InterPro | IPR023333 | Proteasome B-type subunit |
| 1 | 173 | SUPERFAMILY | SSF56235 | N-terminal nucleophile aminohydrolases (Ntn hydrolases) |
| 1 | 173 | InterPro | IPR029055 | Nucleophile aminohydrolases, N-terminal |
| 2 | 173 | CDD | cd01913 | protease_HslV |
| 1 | 173 | ProSiteProfiles | PS51476 | Proteasome beta-type subunit profile. |
| 1 | 173 | InterPro | IPR023333 | Proteasome B-type subunit |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 1Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
PA5053
|
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 | 0.467 |
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.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| LVS | P43772 | 722.6 Da LogP 3.60 TPSA 184.8 | 1 viol. | ✓ Clean |
CC(C)C[C@@H](C=CS(=O)(=O)C)NC(=O)[C@H](CC(C)C)N…
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
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.