Research workbench
AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase (A0KNQ8)
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
- A0KNQ8
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Gamma-glutamyl phosphate reductase
- UniProt
- A0KNQ8
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl phosphate reductase | protein | 417 | 45% helix, 20% strand | A0KNQ8 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 439 | 0.65 | 0.78 | 51 | empty |
| 2 | 107 | 0.38 | 0.75 | 16 | empty |
| 3 | 69 | 0.33 | 0.75 | 17 | empty |
| 4 | 81 | 0.31 | 0.73 | 19 | 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 A0KNQ8
- Elsewhere: UniProt A0KNQ8 · AlphaFold DB A0KNQ8
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