Research workbench
AlphaFold monomer V2.0 prediction for gamma-glutamyl phosphate reductase (B2THG5)
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
- B2THG5
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7b62bBB2fd1BEFAF6006b9Ca6951A38Dfd038f9d
- Molecule
- Gamma-glutamyl phosphate reductase
- UniProt
- B2THG5
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl phosphate reductase | protein | 414 | 47% helix, 20% strand | B2THG5 |
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 | 557 | 0.66 | 0.77 | 48 | empty |
| 2 | 85 | 0.33 | 0.73 | 12 | empty |
| 3 | 82 | 0.31 | 0.73 | 22 | 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 B2THG5
- Elsewhere: UniProt B2THG5 · AlphaFold DB B2THG5
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