Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (B5E5J9)
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
- B5E5J9
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- B5E5J9
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 515 | 42% helix, 20% strand | B5E5J9 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 691 | 0.72 | 0.78 | 60 | empty |
| 2 | 95 | 0.53 | 0.84 | 26 | empty |
| 3 | 127 | 0.52 | 0.81 | 18 | empty |
| 4 | 158 | 0.45 | 0.76 | 20 | empty |
| 5 | 59 | 0.31 | 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 B5E5J9
- Elsewhere: UniProt B5E5J9 · AlphaFold DB B5E5J9
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