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AlphaFold monomer V2.0 prediction for bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (C3XRY1)
Analyse AlphaFold monomer V2.0 prediction for bifunctional lysine-specific demethylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3XRY1
- Type
- protein
- Length
- 607 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe453de7E616d8EC6deB093C9ee2d563d1c020284
- Molecule
- Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66
- UniProt
- C3XRY1
- Pockets
- 7 · best druggability 0.65
Structure
1 distinct chain · 27% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66 | protein | 607 | 27% helix, 15% strand | C3XRY1 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.65 | 0.82 | 50 | empty |
| 2 | 241 | 0.56 | 0.78 | 33 | empty |
| 3 | 136 | 0.50 | 0.80 | 25 | empty |
| 4 | 68 | 0.39 | 0.80 | 19 | empty |
| 5 | 73 | 0.39 | 0.78 | 14 | 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 C3XRY1
- Elsewhere: UniProt C3XRY1 · AlphaFold DB C3XRY1
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