Research workbench
AlphaFold monomer V2.0 prediction for extracellular superoxide dismutase [cu-zn] (P16026)
Analyse AlphaFold monomer V2.0 prediction for extracellular superoxide dismutase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P16026
- Type
- protein
- Length
- 184 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Extracellular superoxide dismutase [cu-zn]
- UniProt
- P16026
Structure
1 distinct chain · 17% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Extracellular superoxide dismutase [cu-zn] | protein | 184 | 17% helix, 34% strand | P16026 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P16026
- Elsewhere: UniProt P16026 · AlphaFold DB P16026
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