Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(P)+] (A1VKS0)
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
- A1VKS0
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a24CBa3fbFCBbB9686CfD21aB7D75cD5a37f2D0
- Molecule
- Glycerol-3-phosphate dehydrogenase [NAD(P)+]
- UniProt
- A1VKS0
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | protein | 352 | 51% helix, 14% strand | A1VKS0 |
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 | 502 | 0.69 | 0.79 | 54 | empty |
| 2 | 196 | 0.58 | 0.80 | 29 | empty |
| 3 | 53 | 0.28 | 0.74 | 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 A1VKS0
- Elsewhere: UniProt A1VKS0 · AlphaFold DB A1VKS0
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