Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (A3Q5N7)
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
- A3Q5N7
- Type
- protein
- Length
- 527 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4B90C51942be0dE1D7B37C1DcDfC4fEd2eCF2c32
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- A3Q5N7
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 527 | 40% helix, 20% strand | A3Q5N7 |
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 | 1119 | 0.72 | 0.76 | 79 | empty |
| 2 | 87 | 0.52 | 0.84 | 24 | empty |
| 3 | 75 | 0.36 | 0.76 | 19 | 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 A3Q5N7
- Elsewhere: UniProt A3Q5N7 · AlphaFold DB A3Q5N7
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