Research workbench
AlphaFold monomer V2.0 prediction for glucans biosynthesis protein C (Q5PGX5)
Analyse AlphaFold monomer V2.0 prediction for glucans biosynthesis protein C (Q5PGX5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5PGX5
- Type
- protein
- Length
- 384 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7F88b78Bd43250971E3B1b401f8c2B17562d5F7C
- Molecule
- Glucans biosynthesis protein C
- UniProt
- Q5PGX5
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucans biosynthesis protein C | protein | 384 | 78% helix, 0% strand | Q5PGX5 |
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 | 622 | 0.72 | 0.79 | 38 | empty |
| 2 | 411 | 0.70 | 0.81 | 42 | empty |
| 3 | 92 | 0.36 | 0.74 | 14 | empty |
| 4 | 89 | 0.36 | 0.74 | 14 | 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 Q5PGX5
- Elsewhere: UniProt Q5PGX5 · AlphaFold DB Q5PGX5
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