Research workbench
AlphaFold monomer V2.0 prediction for bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (B4NP88)
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
- B4NP88
- Type
- protein
- Length
- 767 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb0a2D657Af3Ac4FC3c0675DF7FC17dA77615d32E
- Molecule
- Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66
- UniProt
- B4NP88
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 25% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66 | protein | 767 | 25% helix, 13% strand | B4NP88 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.64 | 0.80 | 55 | empty |
| 2 | 88 | 0.46 | 0.81 | 23 | empty |
| 3 | 87 | 0.34 | 0.74 | 16 | 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 B4NP88
- Elsewhere: UniProt B4NP88 · AlphaFold DB B4NP88
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