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Crystal structure of glutathione reductase GLR1 from the yeast saccharomyces cerevisiae
Analyse Crystal structure of glutathione reductase GLR1 from the yeast saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HQM
- Type
- protein
- Length
- 922 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- EC
- 1.8.1.7
- UniProt
- P41921
- Ligands
- FAD, GSH, NAG, PO4
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutathione reductase (EC 1.8.1.7) | protein | 461 | 35% helix, 26% strand | P41921 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- GSH · Glutathione · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.81 | 0.93 | 33 | empty |
| 2 | 905 | 0.80 | 0.82 | 106 | FAD, GOL |
| 3 | 979 | 0.80 | 0.81 | 114 | FAD, GOL |
| 4 | 652 | 0.69 | 0.77 | 56 | PO4 |
| 5 | 629 | 0.69 | 0.77 | 57 | PO4 |
Interfaces
1 interface between chains.
- A–B · 3560 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 disulfide, 2 glycan (covalent ligand, disulfide, N-glycosylation).
Compared structures
- 2HQM · Crystal Structure of Glutathione Reductase Glr1 from the Yeast Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P41921 · AlphaFold monomer V2.0 prediction for glutathione reductase (P41921) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P41921
- Elsewhere: RCSB PDB 2HQM · PDBe 2HQM · UniProt P41921
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