Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(P)+] (Q7NYZ3)
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
- Q7NYZ3
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Glycerol-3-phosphate dehydrogenase [NAD(P)+]
- UniProt
- Q7NYZ3
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | protein | 334 | 52% helix, 12% strand | Q7NYZ3 |
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 | 438 | 0.74 | 0.84 | 42 | empty |
| 2 | 211 | 0.59 | 0.80 | 30 | empty |
| 3 | 51 | 0.30 | 0.76 | 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 Q7NYZ3
- Elsewhere: UniProt Q7NYZ3 · AlphaFold DB Q7NYZ3
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