Research workbench
AlphaFold monomer V2.0 prediction for N-lysine methyltransferase SMYD2 (E1C5V0)
Analyse AlphaFold monomer V2.0 prediction for N-lysine methyltransferase SMYD2 (E1C5V0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E1C5V0
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE651A2B061FB7771bFB843238E8B9bBBaaA9AbbC
- Molecule
- N-lysine methyltransferase SMYD2
- UniProt
- E1C5V0
- Pockets
- 3 · best druggability 0.79
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-lysine methyltransferase SMYD2 | protein | 436 | 51% helix, 14% strand | E1C5V0 |
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 | 1107 | 0.79 | 0.81 | 103 | empty |
| 2 | 166 | 0.50 | 0.78 | 24 | empty |
| 3 | 71 | 0.44 | 0.81 | 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 E1C5V0
- Elsewhere: UniProt E1C5V0 · AlphaFold DB E1C5V0
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