Research workbench
AlphaFold monomer V2.0 prediction for O-fucosyltransferase 23 (Q9MA87)
Analyse AlphaFold monomer V2.0 prediction for O-fucosyltransferase 23 (Q9MA87) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9MA87
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- O-fucosyltransferase 23
- UniProt
- Q9MA87
- Pockets
- 6 · best druggability 0.66
Structure
1 distinct chain · 42% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-fucosyltransferase 23 | protein | 445 | 42% helix, 13% strand | Q9MA87 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 393 | 0.66 | 0.79 | 36 | empty |
| 2 | 185 | 0.42 | 0.72 | 17 | empty |
| 3 | 103 | 0.37 | 0.75 | 21 | empty |
| 4 | 85 | 0.37 | 0.76 | 17 | empty |
| 5 | 62 | 0.33 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 3 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 Q9MA87
- Elsewhere: UniProt Q9MA87 · AlphaFold DB Q9MA87
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