Research workbench
AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD5 (Q5XJV7)
Analyse AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5XJV7
- Type
- protein
- Length
- 1,441 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9D1b19024D2c9eA9d8eCF531d4acCd9E0a4D782B
- Molecule
- Histone-lysine N-methyltransferase SETD5
- UniProt
- Q5XJV7
- Pockets
- 5 · best druggability 0.69
Structure
1 distinct chain · 11% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SETD5 | protein | 1441 | 11% helix, 4% strand | Q5XJV7 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.69 | 0.82 | 27 | empty |
| 2 | 123 | 0.53 | 0.81 | 24 | empty |
| 3 | 128 | 0.50 | 0.79 | 25 | empty |
| 4 | 96 | 0.45 | 0.80 | 17 | empty |
| 5 | 98 | 0.37 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q5XJV7
- Elsewhere: UniProt Q5XJV7 · AlphaFold DB Q5XJV7
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