Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(P)+] (A7H2I1)
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
- A7H2I1
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Glycerol-3-phosphate dehydrogenase [NAD(P)+]
- UniProt
- A7H2I1
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | protein | 297 | 53% helix, 11% strand | A7H2I1 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.72 | 0.84 | 36 | empty |
| 2 | 176 | 0.59 | 0.81 | 25 | 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 A7H2I1
- Elsewhere: UniProt A7H2I1 · AlphaFold DB A7H2I1
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