Research workbench
AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SMYD3 (Q9CWR2)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SMYD3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CWR2
- Type
- protein
- Length
- 428 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3a113053749Cc34e93243C969a73b8FE780ca633
- Molecule
- Histone-lysine N-methyltransferase SMYD3
- UniProt
- Q9CWR2
- Pockets
- 3 · best druggability 0.80
Structure
1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SMYD3 | protein | 428 | 50% helix, 13% strand | Q9CWR2 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.80 | 0.81 | 105 | empty |
| 2 | 219 | 0.54 | 0.78 | 31 | empty |
| 3 | 191 | 0.48 | 0.76 | 30 | 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 Q9CWR2
- Elsewhere: UniProt Q9CWR2 · AlphaFold DB Q9CWR2
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