Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (B5YLE5)
Analyse AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YLE5
- Type
- protein
- Length
- 522 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6F1477A7ba7b4D12E5dE4da4526a61F2AFaa8749
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- B5YLE5
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 522 | 41% helix, 19% strand | B5YLE5 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 934 | 0.78 | 0.80 | 75 | empty |
| 2 | 105 | 0.52 | 0.83 | 26 | empty |
| 3 | 175 | 0.47 | 0.76 | 22 | empty |
| 4 | 60 | 0.35 | 0.78 | 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 B5YLE5
- Elsewhere: UniProt B5YLE5 · AlphaFold DB B5YLE5
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