Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (A8GZM3)
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
- A8GZM3
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- A8GZM3
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 529 | 37% helix, 20% strand | A8GZM3 |
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 | 1139 | 0.72 | 0.75 | 77 | empty |
| 2 | 113 | 0.50 | 0.81 | 25 | empty |
| 3 | 67 | 0.35 | 0.77 | 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 A8GZM3
- Elsewhere: UniProt A8GZM3 · AlphaFold DB A8GZM3
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