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AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase KMT5C (P0C2N6)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase KMT5C… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0C2N6
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x758850a3D7646b829972912E8A512268C74ceb66
- Molecule
- Histone-lysine N-methyltransferase KMT5C
- UniProt
- P0C2N6
- Pockets
- 8 · best druggability 0.66
Structure
1 distinct chain · 23% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase KMT5C | protein | 470 | 23% helix, 15% strand | P0C2N6 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.66 | 0.83 | 33 | empty |
| 2 | 395 | 0.61 | 0.77 | 42 | empty |
| 3 | 252 | 0.58 | 0.78 | 21 | empty |
| 4 | 245 | 0.55 | 0.77 | 35 | empty |
| 5 | 208 | 0.49 | 0.75 | 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 P0C2N6
- Elsewhere: UniProt P0C2N6 · AlphaFold DB P0C2N6
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