Research workbench
AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD7 (Q4QQN5)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4QQN5
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Histone-lysine N-methyltransferase SETD7
- UniProt
- Q4QQN5
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SETD7 | protein | 366 | 9% helix, 47% strand | Q4QQN5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.44 | 0.75 | 21 | empty |
| 2 | 119 | 0.40 | 0.75 | 20 | empty |
| 3 | 52 | 0.36 | 0.79 | 13 | 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 Q4QQN5
- Elsewhere: UniProt Q4QQN5 · AlphaFold DB Q4QQN5
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