Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(P)+] (B0BXL6)
Analyse AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0BXL6
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9396400046839D06eC319D00A865db2C4c06Cae8
- Molecule
- Glycerol-3-phosphate dehydrogenase [NAD(P)+]
- UniProt
- B0BXL6
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | protein | 338 | 53% helix, 13% strand | B0BXL6 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.72 | 0.82 | 39 | empty |
| 2 | 234 | 0.55 | 0.77 | 30 | empty |
| 3 | 63 | 0.33 | 0.76 | 15 | 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 B0BXL6
- Elsewhere: UniProt B0BXL6 · AlphaFold DB B0BXL6
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