Research workbench
AlphaFold monomer V2.0 prediction for catalase (P30265)
Analyse AlphaFold monomer V2.0 prediction for catalase (P30265) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P30265
- Type
- protein
- Length
- 478 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x904549575bEB2e311D9Afd0Ebf08d60F511A0c5A
- Molecule
- Catalase
- UniProt
- P30265
- Pockets
- 7 · best druggability 0.72
Structure
1 distinct chain · 33% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catalase | protein | 478 | 33% helix, 17% strand | P30265 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 267 | 0.72 | 0.86 | 40 | empty |
| 2 | 333 | 0.64 | 0.80 | 42 | empty |
| 3 | 171 | 0.58 | 0.81 | 30 | empty |
| 4 | 280 | 0.55 | 0.77 | 30 | empty |
| 5 | 72 | 0.32 | 0.75 | 15 | empty |
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 P30265
- Elsewhere: UniProt P30265 · AlphaFold DB P30265
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