Research workbench
AlphaFold monomer V2.0 prediction for protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (Q5NDE8)
Analyse AlphaFold monomer V2.0 prediction for protein O-linked-mannose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5NDE8
- Type
- protein
- Length
- 577 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35612D34a32C306CA4fc1edA9360D1F717e25950
- Molecule
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- UniProt
- Q5NDE8
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 | protein | 577 | 31% helix, 26% strand | Q5NDE8 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 545 | 0.72 | 0.80 | 52 | empty |
| 2 | 235 | 0.51 | 0.76 | 27 | empty |
| 3 | 93 | 0.50 | 0.82 | 17 | empty |
| 4 | 59 | 0.33 | 0.77 | 17 | empty |
| 5 | 83 | 0.33 | 0.74 | 21 | 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 Q5NDE8
- Elsewhere: UniProt Q5NDE8 · AlphaFold DB Q5NDE8
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