Research workbench
AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase (Q04Q92)
Analyse AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q04Q92
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Gamma-glutamyl phosphate reductase
- UniProt
- Q04Q92
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl phosphate reductase | protein | 416 | 46% helix, 19% strand | Q04Q92 |
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 | 586 | 0.69 | 0.79 | 48 | empty |
| 2 | 93 | 0.37 | 0.75 | 16 | empty |
| 3 | 80 | 0.30 | 0.73 | 17 | 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 Q04Q92
- Elsewhere: UniProt Q04Q92 · AlphaFold DB Q04Q92
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