Overview
Basic information about this protein and its source genome.
- Accession
- PA1135
- Gene
- hchA PA1135
- Status
- annotated
- Amino acids
- 291
- Structure source
- AlphaFold
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.
Sequence
Primary amino-acid sequence viewer.
MSNERDTSRTPTPDPAEHNAFFPSPYSLSQYTSAKTDFDGADYPTPYKGGKKVLMIGTDERYILMQNASMFSTGNHPVEMLLPMYHLDKAGFEFDVATLSGNPVKLEMWAMPGEDEAVKSIYAKYLPKLKAPRKLADLLEQAVADDSPYAAVFVPGGHGVLAGIPHSREVKRLLNAFLAKDRYIITLCHGPACLLAPAVEEKPEDYPFKGYEICVFPDALDTGANLEIGYMPGPLPWLVGENLQKLGVKILNKGITGQVHRDRKLLTGDSPLASNNLGKLAAKTLLEAFAR
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
7- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0019172 Catalysis of the reaction: methylglyoxal + H2O = D-lactate.
- GO:0036524 Catalysis of the removal of a sugar or dicarbonyl from a glycated L-arginine, L-lysine or L-cysteine residue within proteins that have been attacked and modified by glyoxal or 2-oxopropanal.
- GO:0016790 Catalysis of the reaction: RCO-SR' + H2O = RCOOH + HSR'. This reaction is the hydrolysis of a thiolester bond, an ester formed from a carboxylic acid and a thiol (i.e., RCO-SR'), such as that found in acetyl-coenzyme A.
- GO:0006281 The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
- GO:0019243 OBSOLETE. The chemical reactions and pathways resulting in the breakdown of methylglyoxal, CH3-CO-CHO, into pyruvate via the intermediate (R)-S-lactoyl-glutathione. Glutathione is used in the first step of the pathway and then regenerated in the second step.
- GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 21 | MobiDBLite | mobidb-lite | consensus disorder prediction |
| 3 | 291 | Hamap | MF_01046 | Protein/nucleic acid deglycase HchA [hchA]. |
| 3 | 291 | InterPro | IPR017283 | Protein/nucleic acid deglycase HchA |
| 51 | 278 | PANTHER | PTHR48094 | PROTEIN/NUCLEIC ACID DEGLYCASE DJ-1-RELATED |
| 1 | 291 | PIRSF | PIRSF037798 | Hsp31 |
| 1 | 291 | InterPro | IPR017283 | Protein/nucleic acid deglycase HchA |
| 2 | 290 | Gene3D | G3DSA:3.40.50.880 | - |
| 2 | 290 | InterPro | IPR029062 | Class I glutamine amidotransferase-like |
| 77 | 196 | Pfam | PF01965 | DJ-1/PfpI family |
| 77 | 196 | InterPro | IPR002818 | DJ-1/PfpI |
| 9 | 286 | SUPERFAMILY | SSF52317 | Class I glutamine amidotransferase-like |
| 9 | 286 | InterPro | IPR029062 | Class I glutamine amidotransferase-like |
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
PA1135
|
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 | 0.673 | ||||||
| 5 | 0.34 |
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.
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.