Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (Q1MA35)
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
- Q1MA35
- Type
- protein
- Length
- 538 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf506A7D0abAEeA4fB2c7941B1a712c251c7EF300
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- Q1MA35
- Pockets
- 6 · best druggability 0.73
Structure
1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 538 | 38% helix, 20% strand | Q1MA35 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.73 | 0.77 | 62 | empty |
| 2 | 144 | 0.57 | 0.83 | 26 | empty |
| 3 | 109 | 0.40 | 0.76 | 16 | empty |
| 4 | 69 | 0.37 | 0.78 | 15 | empty |
| 5 | 124 | 0.35 | 0.72 | 23 | 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 Q1MA35
- Elsewhere: UniProt Q1MA35 · AlphaFold DB Q1MA35
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