Research workbench
AlphaFold monomer V2.0 prediction for glycerol-3-phosphate dehydrogenase [NAD(P)+] (B4RQK9)
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
- B4RQK9
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Glycerol-3-phosphate dehydrogenase [NAD(P)+]
- UniProt
- B4RQK9
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerol-3-phosphate dehydrogenase [NAD(P)+] | protein | 329 | 54% helix, 13% strand | B4RQK9 |
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 | 422 | 0.73 | 0.83 | 44 | empty |
| 2 | 54 | 0.32 | 0.76 | 11 | empty |
| 3 | 53 | 0.32 | 0.77 | 12 | 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 B4RQK9
- Elsewhere: UniProt B4RQK9 · AlphaFold DB B4RQK9
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