Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide N-acetylglucosaminyltransferase 110 kda subunit (Q8CGY8)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8CGY8
- Type
- protein
- Length
- 1,046 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Udp-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kda subunit
- UniProt
- Q8CGY8
- Pockets
- 6 · best druggability 0.72
Structure
1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kda subunit | protein | 1046 | 59% helix, 8% strand | Q8CGY8 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1137 | 0.72 | 0.76 | 84 | empty |
| 2 | 178 | 0.64 | 0.84 | 24 | empty |
| 3 | 136 | 0.45 | 0.76 | 25 | empty |
| 4 | 116 | 0.44 | 0.77 | 26 | empty |
| 5 | 130 | 0.41 | 0.76 | 23 | 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 Q8CGY8
- Elsewhere: UniProt Q8CGY8 · AlphaFold DB Q8CGY8
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