Research workbench
AlphaFold monomer V2.0 prediction for PYRIDOXINE/PYRIDOXAMINE 5'-phosphate oxidase (A5VNZ1)
Analyse AlphaFold monomer V2.0 prediction for PYRIDOXINE/PYRIDOXAMINE 5'-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VNZ1
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- PYRIDOXINE/PYRIDOXAMINE 5'-phosphate oxidase
- UniProt
- A5VNZ1
- Pockets
- 2 · best druggability 0.40
Structure
1 distinct chain · 29% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PYRIDOXINE/PYRIDOXAMINE 5'-phosphate oxidase | protein | 208 | 29% helix, 32% strand | A5VNZ1 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.40 | 0.74 | 18 | empty |
| 2 | 71 | 0.30 | 0.74 | 15 | 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 A5VNZ1
- Elsewhere: UniProt A5VNZ1 · AlphaFold DB A5VNZ1
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