Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (B2G5C2)
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
- B2G5C2
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x05D249E48b5e19C17E7AE90Ad57354470160c428
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- B2G5C2
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 512 | 41% helix, 20% strand | B2G5C2 |
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 | 986 | 0.77 | 0.79 | 62 | empty |
| 2 | 252 | 0.53 | 0.76 | 24 | empty |
| 3 | 94 | 0.48 | 0.82 | 27 | empty |
| 4 | 51 | 0.43 | 0.83 | 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 B2G5C2
- Elsewhere: UniProt B2G5C2 · AlphaFold DB B2G5C2
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