Research workbench
AlphaFold monomer V2.0 prediction for glycolipid sulfotransferase MRA_1383 (A5U275)
Analyse AlphaFold monomer V2.0 prediction for glycolipid sulfotransferase MRA_1383… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5U275
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6f21693d56aA6FE47fEAebd994D4DF52A0B25787
- Molecule
- Glycolipid sulfotransferase MRA_1383
- UniProt
- A5U275
- Pockets
- 4 · best druggability 0.84
Structure
1 distinct chain · 48% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycolipid sulfotransferase MRA_1383 | protein | 326 | 48% helix, 8% strand | A5U275 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 643 | 0.84 | 0.88 | 78 | empty |
| 2 | 52 | 0.60 | 0.93 | 22 | empty |
| 3 | 75 | 0.45 | 0.81 | 22 | empty |
| 4 | 50 | 0.26 | 0.74 | 16 | 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 A5U275
- Elsewhere: UniProt A5U275 · AlphaFold DB A5U275
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