Research workbench
AlphaFold monomer V2.0 prediction for superoxide dismutase [MN/FE] (Q9ZD15)
Analyse AlphaFold monomer V2.0 prediction for superoxide dismutase [MN/FE] (Q9ZD15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9ZD15
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Superoxide dismutase [MN/FE]
- UniProt
- Q9ZD15
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [MN/FE] | protein | 209 | 54% helix, 12% strand | Q9ZD15 |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9ZD15
- Elsewhere: UniProt Q9ZD15 · AlphaFold DB Q9ZD15
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