Overview
Basic information about this protein and its source genome.
- Accession
- KP13_04231
- Gene
- AHE45462.1 hcp
- Status
- annotated
- Amino acids
- 561
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 96.0
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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)
10- GO:0016661 Catalysis of an oxidation-reduction (redox) reaction in which a nitrogenous group, excluding NH and NH2 groups, acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
- GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
- GO:0050418 Catalysis of the reaction: an acceptor + NH4+ + H2O = hydroxylamine + a reduced acceptor + H+.
- GO:0046872 Binding to a metal ion.
- GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
- GO:0042542 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 388 | 559 | Gene3D | G3DSA:3.40.50.2030 | - |
| 388 | 559 | InterPro | IPR016099 | Prismane-like, alpha/beta-sandwich |
| 391 | 559 | FunFam | G3DSA:3.40.50.2030:FF:000001 | Hydroxylamine reductase |
| 243 | 384 | Gene3D | G3DSA:3.40.50.2030 | - |
| 243 | 384 | InterPro | IPR016099 | Prismane-like, alpha/beta-sandwich |
| 243 | 385 | FunFam | G3DSA:3.40.50.2030:FF:000002 | Hydroxylamine reductase |
| 12 | 560 | Hamap | MF_00069 | Hydroxylamine reductase [hcp]. |
| 12 | 560 | InterPro | IPR010048 | Hydroxylamine reductase |
| 12 | 155 | Gene3D | G3DSA:1.20.1270.20 | - |
| 12 | 155 | InterPro | IPR016100 | Prismane, alpha-bundle |
| 12 | 556 | Pfam | PF03063 | Prismane/CO dehydrogenase family |
| 12 | 556 | InterPro | IPR004137 | Hydroxylamine reductase/Ni-containing CO dehydrogenase |
| 12 | 155 | FunFam | G3DSA:1.20.1270.20:FF:000002 | Hydroxylamine reductase |
| 12 | 559 | CDD | cd01914 | HCP |
| 12 | 559 | InterPro | IPR010048 | Hydroxylamine reductase |
| 11 | 559 | SUPERFAMILY | SSF56821 | Prismane protein-like |
| 11 | 559 | InterPro | IPR011254 | Prismane-like superfamily |
| 160 | 243 | FunFam | G3DSA:1.20.1270.20:FF:000001 | Hydroxylamine reductase |
| 12 | 559 | NCBIfam | TIGR01703 | hydroxylamine reductase |
| 7 | 559 | PANTHER | PTHR30109 | HYDROXYLAMINE REDUCTASE |
| 7 | 559 | InterPro | IPR004137 | Hydroxylamine reductase/Ni-containing CO dehydrogenase |
| 161 | 242 | Gene3D | G3DSA:1.20.1270.20 | - |
| 161 | 242 | InterPro | IPR016100 | Prismane, alpha-bundle |
| 12 | 561 | PIRSF | PIRSF000076 | HCP |
| 12 | 561 | InterPro | IPR010048 | Hydroxylamine reductase |
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 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GQL0
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_04231
|
ColabFold | — | — | full sequence | — | Loaded |
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 | 0.994 | ||||||
| 5 | 0.617 | ||||||
| 15 | 0.291 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 4.3 | 0.178 | ||||||
| 2 | 3.73 | 0.143 | ||||||
| 3 | 3.06 | 0.102 | ||||||
| 4 | 2.77 | 0.085 | ||||||
| 5 | 2.19 | 0.052 |
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 | 0.996 | ||||||
| 3 | 0.604 | ||||||
| 11 | 0.365 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 3.69 | 0.14 | ||||||
| 2 | 3.39 | 0.121 | ||||||
| 3 | 3.34 | 0.119 | ||||||
| 4 | 2.28 | 0.057 | ||||||
| 5 | 2.1 | 0.048 |
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.