Research workbench
AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 85A7 (Q9LME8)
Analyse AlphaFold monomer V2.0 prediction for udp-glycosyltransferase 85A7 (Q9LME8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LME8
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB765e36a52DF056e3d74166883b608B9e6599Dd2
- Molecule
- Udp-glycosyltransferase 85A7
- UniProt
- Q9LME8
- Pockets
- 3 · best druggability 0.81
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-glycosyltransferase 85A7 | protein | 487 | 47% helix, 14% strand | Q9LME8 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.81 | 0.86 | 70 | empty |
| 2 | 283 | 0.53 | 0.75 | 41 | empty |
| 3 | 59 | 0.31 | 0.76 | 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 Q9LME8
- Elsewhere: UniProt Q9LME8 · AlphaFold DB Q9LME8
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