Research workbench
AlphaFold monomer V2.0 prediction for histone lysine demethylase PHF8 (P0CH95)
Analyse AlphaFold monomer V2.0 prediction for histone lysine demethylase PHF8 (P0CH95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CH95
- Type
- protein
- Length
- 1,032 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xACf562eCE43b1086A6879785600A6F1cd3014BB9
- Molecule
- Histone lysine demethylase PHF8
- UniProt
- P0CH95
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 22% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone lysine demethylase PHF8 | protein | 1032 | 22% helix, 9% strand | P0CH95 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 702 | 0.76 | 0.81 | 60 | empty |
| 2 | 208 | 0.51 | 0.76 | 22 | empty |
| 3 | 290 | 0.51 | 0.74 | 25 | empty |
| 4 | 78 | 0.31 | 0.73 | 15 | empty |
| 5 | 52 | 0.26 | 0.74 | 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 P0CH95
- Elsewhere: UniProt P0CH95 · AlphaFold DB P0CH95
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