Research workbench
AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (Q5FB29)
Analyse AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (Q5FB29) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5FB29
- Type
- protein
- Length
- 152 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbfB6A20E645a57E7B411A499D089cf9FEe7986C4
- Molecule
- Superoxide dismutase [cu-zn]
- UniProt
- Q5FB29
Structure
1 distinct chain · 6% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] | protein | 152 | 6% helix, 42% strand | Q5FB29 |
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 Q5FB29
- Elsewhere: UniProt Q5FB29 · AlphaFold DB Q5FB29
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