Research workbench
AlphaFold monomer V2.0 prediction for phosphoadenosine 5'-phosphosulfate reductase (B7VI86)
Analyse AlphaFold monomer V2.0 prediction for phosphoadenosine 5'-phosphosulfate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7VI86
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6745126239F03FF6f5d67EEF0C79A02b039C383E
- Molecule
- Phosphoadenosine 5'-phosphosulfate reductase
- UniProt
- B7VI86
- Pockets
- 3 · best druggability 0.82
Structure
1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoadenosine 5'-phosphosulfate reductase | protein | 258 | 48% helix, 14% strand | B7VI86 |
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 | 456 | 0.82 | 0.90 | 46 | empty |
| 2 | 204 | 0.51 | 0.77 | 26 | empty |
| 3 | 101 | 0.38 | 0.76 | 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 B7VI86
- Elsewhere: UniProt B7VI86 · AlphaFold DB B7VI86
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