Research workbench
AlphaFold monomer V2.0 prediction for mannitol-1-phosphate 5-dehydrogenase (A7X522)
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
- A7X522
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB82BBF8d96C5B3247800FA85d8C9E56fE8DbE5c2
- Molecule
- Mannitol-1-phosphate 5-dehydrogenase
- UniProt
- A7X522
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mannitol-1-phosphate 5-dehydrogenase | protein | 368 | 52% helix, 15% strand | A7X522 |
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 | 306 | 0.58 | 0.77 | 33 | empty |
| 2 | 101 | 0.48 | 0.81 | 14 | empty |
| 3 | 69 | 0.32 | 0.75 | 16 | empty |
Compared structures
- 5JNM · Crystal structure of MtlD from Staphylococcus aureus at 1.7-Angstrom resolution · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 5JNM · Crystal structure of mtld from staphylococcus aureus at 1.7-ångström resolution · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 A7X522
- Elsewhere: UniProt A7X522 · AlphaFold DB A7X522
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