Research workbench
AlphaFold monomer V2.0 prediction for modification methylase hgidii (P25265)
Analyse AlphaFold monomer V2.0 prediction for modification methylase hgidii (P25265) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25265
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Modification methylase hgidii
- UniProt
- P25265
- Pockets
- 2 · best druggability 0.65
Structure
1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Modification methylase hgidii | protein | 354 | 39% helix, 16% strand | P25265 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 486 | 0.65 | 0.78 | 57 | empty |
| 2 | 67 | 0.28 | 0.73 | 19 | 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 P25265
- Elsewhere: UniProt P25265 · AlphaFold DB P25265
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