Research workbench
AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase setmar (Q5I0M0)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase setmar… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5I0M0
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x373207Fe3421B2805A883DB60Ad7660263f6d3ea
- Molecule
- Histone-lysine N-methyltransferase setmar
- UniProt
- Q5I0M0
- Pockets
- 6 · best druggability 0.79
Structure
1 distinct chain · 9% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase setmar | protein | 315 | 9% helix, 22% strand | Q5I0M0 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 870 | 0.79 | 0.82 | 83 | empty |
| 2 | 318 | 0.61 | 0.78 | 33 | empty |
| 3 | 120 | 0.49 | 0.80 | 20 | empty |
| 4 | 110 | 0.46 | 0.79 | 25 | empty |
| 5 | 103 | 0.39 | 0.76 | 18 | 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 Q5I0M0
- Elsewhere: UniProt Q5I0M0 · AlphaFold DB Q5I0M0
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