Research workbench
AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SUVR5 (O64827)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SUVR5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O64827
- Type
- protein
- Length
- 1,382 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- Histone-lysine N-methyltransferase SUVR5
- UniProt
- O64827
- Pockets
- 20 · best druggability 0.69
Structure
1 distinct chain · 23% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SUVR5 | protein | 1382 | 23% helix, 10% strand | O64827 |
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 374 | 0.69 | 0.82 | 54 | empty |
| 2 | 656 | 0.67 | 0.76 | 64 | empty |
| 3 | 239 | 0.61 | 0.80 | 33 | empty |
| 4 | 166 | 0.58 | 0.81 | 26 | empty |
| 5 | 198 | 0.51 | 0.77 | 20 | 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 O64827
- Elsewhere: UniProt O64827 · AlphaFold DB O64827
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