Research workbench
AlphaFold monomer V2.0 prediction for bifunctional purine biosynthesis protein purh (B2HEC3)
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
- B2HEC3
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8EFd901A9417Db3E794c277E751d8219022562Ec
- Molecule
- Bifunctional purine biosynthesis protein purh
- UniProt
- B2HEC3
- Pockets
- 5 · best druggability 0.71
Structure
1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional purine biosynthesis protein purh | protein | 523 | 41% helix, 20% strand | B2HEC3 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.71 | 0.79 | 51 | empty |
| 2 | 370 | 0.61 | 0.77 | 43 | empty |
| 3 | 83 | 0.51 | 0.84 | 27 | empty |
| 4 | 100 | 0.36 | 0.74 | 18 | empty |
| 5 | 67 | 0.29 | 0.74 | 16 | 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 B2HEC3
- Elsewhere: UniProt B2HEC3 · AlphaFold DB B2HEC3
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