Research workbench
AlphaFold monomer V2.0 prediction for superoxide dismutase [mn] (P54375)
Analyse AlphaFold monomer V2.0 prediction for superoxide dismutase [mn] (P54375) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P54375
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Superoxide dismutase [mn]
- UniProt
- P54375
- Pockets
- 1 · best druggability 0.35
Structure
1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [mn] | protein | 202 | 53% helix, 12% strand | P54375 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.35 | 0.76 | 17 | empty |
Compared structures
- 2RCV · Crystal structure of the Bacillus subtilis superoxide dismutase · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 2RCV · Crystal structure of the bacillus subtilis superoxide dismutase · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P54375
- Elsewhere: UniProt P54375 · AlphaFold DB P54375
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