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Ligands
Code Name Style Show Link
FAD Flavin-adenine dinucleotide
PO4 Phosphate ion
Non-standard Residues
Code Name Show
0A8 S-[(2-chloroethyl)carbamoyl]-L-cysteine
Glycosylation
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Code : 1GRG   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE(FLAVOENZYME)
Title : SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION
Release Data : 1994-01-31
Compound :
mol_id molecule chains
1 GLUTATHIONE REDUCTASE A
ec: 1.6.4.2
Source :
mol_id organism_scientific organism_common
1 Homo sapiens  (taxid:9606) Human
Authors : Karplus, P.A., Schulz, G.E.
Keywords : OXIDOREDUCTASE(FLAVOENZYME)
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.

Karplus, P.A.,Schulz, G.E.
(1989)  J.Mol.Biol.  210 : 163 - 180

PubMed: 2585516
DOI: 10.1016/0022-2836(89)90298-2

Inhibition of Human Glutathione Reductase by the Nitrosourea Drugs 1,3-Bis(2-Chloroethyl)-1-Nitrosourea and 1-(2-Chloroethyl)-3-(2-Hydroxyethyl)-1-Nitrosourea

Karplus, P.A.,Krauth-Siegel, R.L.,Schirmer, R.H.  et al.
(1988)  Eur.J.Biochem.  171 : 193

Refined Structure of Glutathione Reductase at 1.54 Angstroms Resolution

Karplus, P.A.,Schulz, G.E.
(1987)  J.Mol.Biol.  195 : 701

Interaction of a Glutathione S-Conjugate with Glutathione Reductase. Kinetic and X-Ray Crystallographic Studies

Bilzer, M.,Krauth-Siegel, R.L.,Schirmer, R.H.  et al.
(1984)  Eur.J.Biochem.  138 : 373

Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase

Wierenga, R.K.,Drenth, J.,Schulz, G.E.
(1983)  J.Mol.Biol.  167 : 725

The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates

Pai, E.F.,Schulz, G.E.
(1983)  J.Biol.Chem.  258 : 1752

Fad-Binding Site of Glutathione Reductase

Schulz, G.E.,Schirmer, R.H.,Pai, E.F.
(1982)  J.Mol.Biol.  160 : 287

Glutathione Reductase from Human Erythrocytes. The Sequences of the Nadph Domain and of the Interface Domain

Krauth-Siegel, R.L.,Blatterspiel, R.,Saleh, M.  et al.
(1982)  Eur.J.Biochem.  121 : 259

Three-Dimensional Structure of Glutathione Reductase at 2 Angstroms Resolution

Thieme, R.,Pai, E.F.,Schirmer, R.H.  et al.
(1981)  J.Mol.Biol.  152 : 763

Gene Duplication in Glutathione Reductase

Schulz, G.E.
(1980)  J.Mol.Biol.  138 : 335

The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine

Untucht-Grau, R.,Schulz, G.E.,Schirmer, R.H.
(1979)  FEBS Lett.  105 : 244

The Structure of the Flavoenzyme Glutathione Reductase

Schulz, G.E.,Schirmer, R.H.,Sachsenheimer, W.  et al.
(1978)  Nature  273 : 120

Low Resolution Structure of Human Erythrocyte Glutathione Reductase

Zappe, H.A.,Krohne-Ehrich, G.,Schulz, G.E.
(1977)  J.Mol.Biol.  113 : 141

Crystals of Human Erythrocyte Glutathione Reductase

Schulz, G.E.,Zappe, H.,Worthington, D.J.  et al.
(1975)  FEBS Lett.  54 : 86

Chain : A
UniProt : P00390 (GSHR_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH 1.8.1.7 PubMed:17185460
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