Overview
Basic information about this protein and its source genome.
- Accession
- KP13_02962
- Gene
- AHE42419.1
- Status
- annotated
- Amino acids
- 338
- 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
- Periplasmic
- ColabFold pLDDT
- 88.25
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)
6- GO:0016667 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
- GO:0030091 The process of restoring a protein to its original state after damage by such things as oxidation or spontaneous decomposition of residues.
- GO:0043546 Binding to a molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands.
- GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
- GO:0046872 Binding to a metal ion.
- GO:0016672 Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces quinone or a related compound.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 32 | Phobius | SIGNAL_PEPTIDE_N_REGION | N-terminal region of a signal peptide. |
| 49 | 338 | Phobius | NON_CYTOPLASMIC_DOMAIN | Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region. |
| 68 | 338 | Gene3D | G3DSA:3.90.420.10 | - |
| 68 | 338 | InterPro | IPR036374 | Oxidoreductase, molybdopterin-binding domain superfamily |
| 1 | 48 | ProSiteProfiles | PS51318 | Twin arginine translocation (Tat) signal profile. |
| 1 | 48 | InterPro | IPR006311 | Twin-arginine translocation pathway, signal sequence |
| 89 | 306 | CDD | cd02107 | YedY_like_Moco |
| 9 | 338 | Hamap | MF_01206 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP [msrP]. |
| 9 | 338 | InterPro | IPR022867 | Protein-methionine-sulfoxide reductase subunit MsrP |
| 33 | 42 | Phobius | SIGNAL_PEPTIDE_H_REGION | Hydrophobic region of a signal peptide. |
| 113 | 271 | Pfam | PF00174 | Oxidoreductase molybdopterin binding domain |
| 113 | 271 | InterPro | IPR000572 | Oxidoreductase, molybdopterin-binding domain |
| 43 | 48 | Phobius | SIGNAL_PEPTIDE_C_REGION | C-terminal region of a signal peptide. |
| 1 | 48 | Phobius | SIGNAL_PEPTIDE | Signal peptide region |
| 12 | 333 | PANTHER | PTHR43032 | PROTEIN-METHIONINE-SULFOXIDE REDUCTASE |
| 80 | 334 | SUPERFAMILY | SSF56524 | Oxidoreductase molybdopterin-binding domain |
| 80 | 334 | InterPro | IPR036374 | Oxidoreductase, molybdopterin-binding 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.
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_A0A0H3GZ50
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02962
|
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 | 0.949 | ||||||
| 18 | 0.589 | ||||||
| 11 | 0.407 |
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 | 20.84 | 0.863 | ||||||
| 2 | 5.27 | 0.247 | ||||||
| 3 | 4.0 | 0.159 | ||||||
| 4 | 2.51 | 0.07 |
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 | 0.981 | ||||||
| 15 | 0.484 |
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 | 26.35 | 0.913 | ||||||
| 2 | 7.53 | 0.397 | ||||||
| 3 | 3.21 | 0.111 |
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 |
|---|---|---|---|---|---|---|
| MO | P76342 | 95.9 Da LogP -0.00 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
[Mo]
|
|
| MSS | Q9LA16 | 505.3 Da LogP -0.12 TPSA 188.9 | 3 viol. | ✓ Clean |
C([C@@H]1C2=C([C@H]3[C@@H](O1)NC4=C(N3)C(=O)NC(…
|
|
| MTE | P76342 | 395.4 Da LogP -0.54 TPSA 171.8 | 1 viol. | ✓ Clean |
C([C@@H]1C(=C([C@H]2[C@@H](O1)NC3=C(N2)C(=O)NC(…
|
|
| O | P76342 | 18.0 Da LogP -0.82 TPSA 31.5 | ✓ Ro5 | ✓ Clean |
O
|
|
| W | P76342 | 183.8 Da LogP -0.00 TPSA 0.0 | ✓ Ro5 | ✓ Clean |
[W+6]
|
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.