Research workbench
AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 75D1 (O23406)
Analyse AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 75D1 (O23406) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O23406
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB765e36a52DF056e3d74166883b608B9e6599Dd2
- Molecule
- Udp-glycosyltransferase 75D1
- UniProt
- O23406
- Pockets
- 4 · best druggability 0.84
Structure
1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glycosyltransferase 75D1 | protein | 474 | 46% helix, 15% strand | O23406 |
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 | 929 | 0.84 | 0.85 | 68 | empty |
| 2 | 619 | 0.68 | 0.77 | 53 | empty |
| 3 | 91 | 0.42 | 0.78 | 26 | empty |
| 4 | 52 | 0.34 | 0.78 | 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 O23406
- Elsewhere: UniProt O23406 · AlphaFold DB O23406
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