Research workbench
AlphaFold monomer V2.0 prediction for N-lysine methyltransferase SETD6 (A4QNG5)
Analyse AlphaFold monomer V2.0 prediction for N-lysine methyltransferase SETD6 (A4QNG5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4QNG5
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- N-lysine methyltransferase SETD6
- UniProt
- A4QNG5
- Pockets
- 9 · best druggability 0.56
Structure
1 distinct chain · 46% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-lysine methyltransferase SETD6 | protein | 454 | 46% helix, 11% strand | A4QNG5 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.56 | 0.76 | 42 | empty |
| 2 | 162 | 0.54 | 0.80 | 30 | empty |
| 3 | 121 | 0.42 | 0.76 | 25 | empty |
| 4 | 77 | 0.37 | 0.77 | 15 | empty |
| 5 | 131 | 0.37 | 0.73 | 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 A4QNG5
- Elsewhere: UniProt A4QNG5 · AlphaFold DB A4QNG5
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