Research workbench
AlphaFold monomer V2.0 prediction for protein O-glucosyltransferase 1 (Q5E9Q1)
Analyse AlphaFold monomer V2.0 prediction for protein O-glucosyltransferase 1 (Q5E9Q1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5E9Q1
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe26BC75B33Cf508D508699DA6F01356e8b386510
- Molecule
- Protein O-glucosyltransferase 1
- UniProt
- Q5E9Q1
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein O-glucosyltransferase 1 | protein | 392 | 39% helix, 15% strand | Q5E9Q1 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.74 | 0.85 | 35 | empty |
| 2 | 60 | 0.34 | 0.78 | 14 | empty |
| 3 | 59 | 0.34 | 0.77 | 17 | empty |
| 4 | 57 | 0.32 | 0.77 | 17 | empty |
| 5 | 51 | 0.27 | 0.74 | 10 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q5E9Q1
- Elsewhere: UniProt Q5E9Q1 · AlphaFold DB Q5E9Q1
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