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The structure of glutathione reductase from escherichia COLI at 1.86 ångströms resolution: comparison with the enzyme from human erythrocytes
Analyse The structure of glutathione reductase from escherichia COLI at 1.86 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GER
- Type
- protein
- Length
- 897 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione reductase
- EC
- 1.6.4.2
- UniProt
- P06715
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione reductase (EC 1.6.4.2) | protein | 448 | 36% helix, 27% strand | P06715 |
| B | Glutathione reductase (EC 1.6.4.2) | protein | 449 | 36% helix, 27% strand | P06715 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.87 | 0.88 | 139 | empty |
| 2 | 741 | 0.78 | 0.82 | 98 | FAD |
| 3 | 722 | 0.78 | 0.82 | 87 | FAD |
| 4 | 56 | 0.44 | 0.84 | 19 | empty |
| 5 | 52 | 0.29 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3473 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1GER · The structure of glutathione reductase from escherichia COLI at 1.86 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
- P06715 · AlphaFold monomer V2.0 prediction for glutathione reductase (P06715) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 P06715
- Elsewhere: RCSB PDB 1GER · PDBe 1GER · UniProt P06715
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