Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (B7K3N8)
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
- B7K3N8
- Type
- protein
- Length
- 516 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- B7K3N8
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 516 | 41% helix, 21% strand | B7K3N8 |
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 | 586 | 0.66 | 0.76 | 52 | empty |
| 2 | 359 | 0.55 | 0.74 | 40 | empty |
| 3 | 70 | 0.39 | 0.79 | 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 B7K3N8
- Elsewhere: UniProt B7K3N8 · AlphaFold DB B7K3N8
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