Research workbench
AlphaFold monomer V2.0 prediction for xanthine dehydrogenase (P91711)
Analyse AlphaFold monomer V2.0 prediction for xanthine dehydrogenase (P91711) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P91711
- Type
- protein
- Length
- 1,344 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Xanthine dehydrogenase
- UniProt
- P91711
- Pockets
- 19 · best druggability 0.85
Structure
1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xanthine dehydrogenase | protein | 1344 | 33% helix, 23% strand | P91711 |
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 900 | 0.85 | 0.87 | 82 | empty |
| 2 | 579 | 0.79 | 0.85 | 60 | empty |
| 3 | 459 | 0.79 | 0.86 | 75 | empty |
| 4 | 362 | 0.74 | 0.85 | 44 | empty |
| 5 | 58 | 0.73 | 0.99 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P91711
- Elsewhere: UniProt P91711 · AlphaFold DB P91711
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