Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (Q8NS21)
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
- Q8NS21
- Type
- protein
- Length
- 520 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd7BceDA0b55dbEde1C94d30aA0d6409be898E5bF
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- Q8NS21
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 520 | 42% helix, 20% strand | Q8NS21 |
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 | 892 | 0.71 | 0.76 | 79 | empty |
| 2 | 123 | 0.56 | 0.83 | 26 | empty |
| 3 | 201 | 0.47 | 0.74 | 25 | empty |
| 4 | 109 | 0.40 | 0.76 | 17 | 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 Q8NS21
- Elsewhere: UniProt Q8NS21 · AlphaFold DB Q8NS21
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