Research workbench
AlphaFold monomer V2.0 prediction for protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (Q5NDE7)
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
- Q5NDE7
- Type
- protein
- Length
- 578 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF1437035F7890bd590E2820a667B75cf387314Ef
- Molecule
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- UniProt
- Q5NDE7
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 | protein | 578 | 32% helix, 25% strand | Q5NDE7 |
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 | 485 | 0.70 | 0.80 | 48 | empty |
| 2 | 202 | 0.48 | 0.75 | 28 | empty |
| 3 | 70 | 0.43 | 0.81 | 17 | empty |
| 4 | 75 | 0.31 | 0.74 | 17 | empty |
| 5 | 59 | 0.29 | 0.74 | 12 | 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 Q5NDE7
- Elsewhere: UniProt Q5NDE7 · AlphaFold DB Q5NDE7
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