Overview
Basic information about this protein and its source genome.
- Accession
- KP13_05143
- Gene
- sodB AHE44262.1
- Status
- annotated
- Amino acids
- 193
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 58.333
- Human E-value
- 2.27e-07
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 70.466
- DEG E-value
- 3.85e-101
- Localization
- Periplasmic
- ColabFold pLDDT
- 98.19
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)
5- GO:0004784 Catalysis of the reaction: 2 superoxide + 2 H+ = O2 + H2O2.
- GO:0006801 The chemical reactions and pathways involving superoxide, the superoxide anion O2- (superoxide free radical), or any compound containing this species.
- GO:0046872 Binding to a metal ion.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0046914 Binding to a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 1 | 193 | PIRSF | PIRSF000349 | MnSOD_FeSOD |
| 1 | 193 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 20 | 81 | FunFam | G3DSA:1.10.287.990:FF:000002 | Superoxide dismutase |
| 157 | 164 | ProSitePatterns | PS00088 | Manganese and iron superoxide dismutases signature. |
| 157 | 164 | InterPro | IPR019833 | Manganese/iron superoxide dismutase, binding site |
| 6 | 17 | PRINTS | PR01703 | Manganese superoxide dismutase signature |
| 6 | 17 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 155 | 167 | PRINTS | PR01703 | Manganese superoxide dismutase signature |
| 155 | 167 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 118 | 126 | PRINTS | PR01703 | Manganese superoxide dismutase signature |
| 118 | 126 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 27 | 40 | PRINTS | PR01703 | Manganese superoxide dismutase signature |
| 27 | 40 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 65 | 78 | PRINTS | PR01703 | Manganese superoxide dismutase signature |
| 65 | 78 | InterPro | IPR001189 | Manganese/iron superoxide dismutase |
| 2 | 82 | Pfam | PF00081 | Iron/manganese superoxide dismutases, alpha-hairpin domain |
| 2 | 82 | InterPro | IPR019831 | Manganese/iron superoxide dismutase, N-terminal |
| 82 | 193 | FunFam | G3DSA:3.55.40.20:FF:000001 | Superoxide dismutase |
| 81 | 193 | Gene3D | G3DSA:3.55.40.20 | - |
| 81 | 193 | InterPro | IPR036314 | Manganese/iron superoxide dismutase, C-terminal domain superfamily |
| 82 | 191 | SUPERFAMILY | SSF54719 | Fe,Mn superoxide dismutase (SOD), C-terminal domain |
| 82 | 191 | InterPro | IPR036314 | Manganese/iron superoxide dismutase, C-terminal domain superfamily |
| 89 | 189 | Pfam | PF02777 | Iron/manganese superoxide dismutases, C-terminal domain |
| 89 | 189 | InterPro | IPR019832 | Manganese/iron superoxide dismutase, C-terminal |
| 3 | 192 | PANTHER | PTHR42769 | SUPEROXIDE DISMUTASE |
| 1 | 84 | SUPERFAMILY | SSF46609 | Fe,Mn superoxide dismutase (SOD), N-terminal domain |
| 1 | 84 | InterPro | IPR036324 | Manganese/iron superoxide dismutase, N-terminal domain superfamily |
| 20 | 80 | Gene3D | G3DSA:1.10.287.990 | Fe,Mn superoxide dismutase (SOD) domain |
| 20 | 80 | InterPro | IPR036324 | Manganese/iron superoxide dismutase, N-terminal 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_A0A0H3GYY6
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_05143
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
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 | 1.39 | 0.017 | ||||||
| 2 | 1.31 | 0.014 |
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 |
|---|---|---|---|---|---|---|---|
| 6 | 0.26 | ||||||
| 4 | 0.237 |
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 | 1.47 | 0.02 |
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 |
|---|---|---|---|---|---|---|
| AZI | P0AGD3 | 42.0 Da LogP 0.87 TPSA 58.7 | ✓ Ro5 | Alert |
[N-]=[N+]=[N-]
|
|
| MH2 | P00448 | 71.9 Da LogP -0.56 TPSA 20.2 | ✓ Ro5 | ✓ Clean |
O[Mn+2]
|
|
| MLI | P41977 | 102.0 Da LogP -3.12 TPSA 80.3 | ✓ Ro5 | ✓ Clean |
C(C(=O)[O-])C(=O)[O-]
|
|
| O | P0AGD3 | 18.0 Da LogP -0.82 TPSA 31.5 | ✓ Ro5 | ✓ Clean |
O
|
|
| PEO | P00448 | 34.0 Da LogP 0.02 TPSA 40.5 | ✓ Ro5 | ✓ Clean |
OO
|
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.