Research workbench
AlphaFold monomer V2.0 prediction for modification methylase hgicii (P25264)
Analyse AlphaFold monomer V2.0 prediction for modification methylase hgicii (P25264) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P25264
- Type
- protein
- Length
- 437 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x869cF49c6E985236b321a48Bc767b1Af062c4598
- Molecule
- Modification methylase hgicii
- UniProt
- P25264
- Pockets
- 5 · best druggability 0.60
Structure
1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Modification methylase hgicii | protein | 437 | 34% helix, 18% strand | P25264 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.60 | 0.79 | 39 | empty |
| 2 | 110 | 0.57 | 0.85 | 23 | empty |
| 3 | 220 | 0.52 | 0.77 | 38 | empty |
| 4 | 169 | 0.49 | 0.77 | 25 | empty |
| 5 | 71 | 0.39 | 0.79 | 16 | 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 P25264
- Elsewhere: UniProt P25264 · AlphaFold DB P25264
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