Research workbench
AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P0AGD1)
Analyse AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (P0AGD1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0AGD1
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0E5d19AAbEf43d610964131Fe6042A63EE0dd81A
- Molecule
- Superoxide dismutase [cu-zn]
- UniProt
- P0AGD1
- Pockets
- 1 · best druggability 0.29
Structure
1 distinct chain · 5% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Superoxide dismutase [cu-zn] | protein | 173 | 5% helix, 39% strand | P0AGD1 |
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 | 70 | 0.29 | 0.73 | 16 | empty |
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 P0AGD1
- Elsewhere: UniProt P0AGD1 · AlphaFold DB P0AGD1
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