Research workbench
AlphaFold monomer V2.0 prediction for mannitol-1-phosphate 5-dehydrogenase (B1JH11)
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
- B1JH11
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Mannitol-1-phosphate 5-dehydrogenase
- UniProt
- B1JH11
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannitol-1-phosphate 5-dehydrogenase | protein | 387 | 55% helix, 15% strand | B1JH11 |
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 | 488 | 0.71 | 0.81 | 45 | empty |
| 2 | 56 | 0.30 | 0.75 | 12 | empty |
| 3 | 60 | 0.28 | 0.73 | 13 | 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 B1JH11
- Elsewhere: UniProt B1JH11 · AlphaFold DB B1JH11
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