[English] 日本語
![](img/lk-miru.gif)
- PDB-4gr1: THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLU... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4gr1 | ||||||
---|---|---|---|---|---|---|---|
Title | THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE | ||||||
![]() | GLUTATHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE (FLAVOENZYME) | ||||||
Function / homology | ![]() glutathione-disulfide reductase / Metabolism of ingested H2SeO4 and H2SeO3 into H2Se / glutathione-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / NFE2L2 regulating anti-oxidant/detoxification enzymes / Detoxification of Reactive Oxygen Species / glutathione metabolic process / cell redox homeostasis / TP53 Regulates Metabolic Genes / NADP binding ...glutathione-disulfide reductase / Metabolism of ingested H2SeO4 and H2SeO3 into H2Se / glutathione-disulfide reductase (NADPH) activity / Interconversion of nucleotide di- and triphosphates / NFE2L2 regulating anti-oxidant/detoxification enzymes / Detoxification of Reactive Oxygen Species / glutathione metabolic process / cell redox homeostasis / TP53 Regulates Metabolic Genes / NADP binding / flavin adenine dinucleotide binding / cellular response to oxidative stress / electron transfer activity / mitochondrial matrix / external side of plasma membrane / mitochondrion / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schulz, G.E. / Janes, W. | ||||||
![]() | ![]() Title: The binding of the retro-analogue of glutathione disulfide to glutathione reductase. Authors: Janes, W. / Schulz, G.E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 117.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 88.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: RESIDUES PRO 375 AND PRO 468 ARE CIS PROLINES. 2: CYS 90 FORMS A DISULFIDE BRIDGE WITH ITS COUNTERPART IN THE OTHER SUBUNIT. SEE REMARK 4 ABOVE FOR THE TRANSFORMATION T GENERATE THIS SECOND SUBUNIT. 3: DISCRETE DISORDER WAS OBSERVED FOR RESIDUES 20, 99, 119, 190, 202, 231, 276, 292, 373, 406, 420, AND 457. 4: A DISULFIDE BOND IS FORMED BETWEEN ATOMS SG AND SG* OF THE RETRO-GSSG (RGS 481) GROUP. | ||||||||
Details | GLUTATHIONE REDUCTASE IS ACTIVE AS A DIMER OF TWO IDENTICAL SUBUNITS. THE SECOND SUBUNIT CAN BE GENERATED FROM THE ONE PRESENTED IN THIS ENTRY BY THE FOLLOWING TRANSFORMATION: XPRIME = 163.6994 - X YPRIME = 72.2018 - Y |
-
Components
#1: Protein | Mass: 51636.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|---|
#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-FAD / |
#4: Chemical | ChemComp-RGS / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.51 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: referred to J.Mol.Biol.152.763-782 | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 21690 |
---|
-
Processing
Software | Name: TNT / Classification: refinement | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor obs: 0.151 / Highest resolution: 2.4 Å Details: DISCRETE DISORDER WAS OBSERVED FOR RESIDUES 20, 99, 119, 190, 202, 231, 276, 292, 373, 406, 420, AND 457. | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
|