Research workbench
AlphaFold monomer V2.0 prediction for mannitol-1-phosphate 5-dehydrogenase (Q7SA44)
Analyse AlphaFold monomer V2.0 prediction for mannitol-1-phosphate 5-dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7SA44
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb9595fEff3a9863942Eb06A0EA3017ECa562408c
- Molecule
- Mannitol-1-phosphate 5-dehydrogenase
- UniProt
- Q7SA44
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 51% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannitol-1-phosphate 5-dehydrogenase | protein | 398 | 51% helix, 15% strand | Q7SA44 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.72 | 0.81 | 41 | empty |
| 2 | 78 | 0.33 | 0.74 | 11 | empty |
| 3 | 72 | 0.31 | 0.74 | 15 | empty |
| 4 | 50 | 0.28 | 0.75 | 14 | 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 Q7SA44
- Elsewhere: UniProt Q7SA44 · AlphaFold DB Q7SA44
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