Research workbench
AlphaFold monomer V2.0 prediction for arginine-hydroxylase NDUFAF5, mitochondrial (B2GV71)
Analyse AlphaFold monomer V2.0 prediction for arginine-hydroxylase NDUFAF5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B2GV71
- Type
- protein
- Length
- 343 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- Arginine-hydroxylase NDUFAF5, mitochondrial
- UniProt
- B2GV71
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine-hydroxylase NDUFAF5, mitochondrial | protein | 343 | 33% helix, 22% strand | B2GV71 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.70 | 0.98 | 27 | empty |
| 2 | 150 | 0.55 | 0.81 | 20 | empty |
| 3 | 112 | 0.40 | 0.76 | 24 | 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 B2GV71
- Elsewhere: UniProt B2GV71 · AlphaFold DB B2GV71
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