Research workbench
AlphaFold monomer V2.0 prediction for mannose-1-phosphate guanyltransferase 1 (Q9Y725)
Analyse AlphaFold monomer V2.0 prediction for mannose-1-phosphate guanyltransferase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9Y725
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Mannose-1-phosphate guanyltransferase 1
- UniProt
- Q9Y725
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 26% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannose-1-phosphate guanyltransferase 1 | protein | 361 | 26% helix, 32% strand | Q9Y725 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.56 | 0.77 | 35 | empty |
| 2 | 145 | 0.47 | 0.77 | 21 | empty |
| 3 | 66 | 0.42 | 0.81 | 18 | 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 Q9Y725
- Elsewhere: UniProt Q9Y725 · AlphaFold DB Q9Y725
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