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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P00390 New Search
27PDB entries
27Biological assembly
29chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1ALG SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES Deposited 1997-06-03 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 436–459（24 aa） Fragment：INTERSUBUNIT-CONTACT HELIX
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.1；283 K
Resolution not provided
1BWC STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE Deposited 1998-09-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded CL CHLORIDE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 AJ3 3-(PROP-2-ENE-1-SULFINYL)-PROPENE-1-THIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9；pH 6.9
Resolution 2.10 Å R-free 0.230
1DNC HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON Deposited 1998-02-20 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å R-free 0.248
1GRA SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 GSH Glutathione × 4 X-RAY DIFFRACTION
X-ray crystallization conditions THE ENZYME CRYSTAL WAS SOAKED WITH GSSG AND NADP+, DATA WERE COLLECTED, AND THE STRUCTURE OF THE OXIDIZED ENZYME WITH BOUND GSSG AND NADP+ WAS REFINED. THE STRUCTURE CONTAINS 530 WATER MOLECULES, 38 DELETED IN RELATION TO FILE 3GRS, 45 ADDED IN RELATION TO FILE 3GRS.
Resolution 2.00 Å
1GRB SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.85 Å
1GRE SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1GRF SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ACM ACETAMIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1GRG SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1GRH 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 Deposited 1992-12-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EOH ETHANOL × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 3.00 Å
1GRT HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT Deposited 1996-12-17 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Mutation：A34E, R37W FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；0.57-0.90 M AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION, vapor diffusion - hanging drop
Resolution 2.30 Å
1GSN HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE Deposited 1998-02-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.70 Å R-free 0.249
1K4Q Human Glutathione Reductase Inactivated by Peroxynitrite Deposited 2001-10-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 62–522（461 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Ammonium Sulfate, Potassium Phosphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.204
1XAN HUMAN GLUTATHIONE REDUCTASE IN COMPLEX WITH A XANTHENE INHIBITOR Deposited 1996-01-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 18–478（461 aa）
Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 HXP 3,6-DIHYDROXY-XANTHENE-9-PROPIONIC ACID × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
2AAQ Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI Deposited 2005-07-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 44–522（479 aa）
Not recorded PO4 PHOSPHATE ION × 8 CL CHLORIDE ION × 2 K POTASSIUM ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 AUP 2-(2-PHENYL-3-PYRIDIN-2-YL-4,5,6,7-TETRAHYDRO-2H-ISOPHOSPHINDOL-1-YL)PYRIDINE × 2 AU GOLD ION × 4 GOL GLYCEROL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.60 Å R-free 0.259
2GH5 Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5 Deposited 2006-03-25 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa） Fragment：glutathione reductase
Chain B 45–522（478 aa） Fragment：glutathione reductase
Not recorded PO4 PHOSPHATE ION × 4 ELI 6-(3-METHYL-1,4-DIOXO-1,4-DIHYDRONAPHTHALEN-2-YL)HEXANOIC ACID × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100 mM potassium phosphate, pH 8.0 and 16% NH4SO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.256
2GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX Deposited 1997-02-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 18–478（461 aa）
Mutation：A34E, R37W FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GDS OXIDIZED GLUTATHIONE DISULFIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；0.57-0.90 M AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION. CRYSTALS WERE SOAKED IN ARTIFICIAL MOTHER LIQUOR AT PH 6.5 420, vapor diffusion - hanging drop
Resolution 2.70 Å
3DJG Catalytic cycle of human glutathione reductase near 1 A resolution Deposited 2008-06-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain X 62–522（461 aa） Fragment：UNP residues 45 to 522
Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；298 K；3% ammonium sulfate, 0.1 M potassium phosphate and 0.1% beta-octyl glucoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00
Resolution 1.80 Å R-free 0.186
3DJJ Catalytic cycle of human glutathione reductase near 1 A resolution Deposited 2008-06-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa） Fragment：UNP residues 45 to 522
Not recorded PO4 PHOSPHATE ION × 10 SO4 SULFATE ION × 8 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 GOL GLYCEROL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；298 K；3% ammonium sulfate, 0.1 M potassium phosphate and 0.1% beta-octyl glucoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00
Resolution 1.10 Å R-free 0.147
3DK4 Catalytic cycle of human glutathione reductase near 1 A resolution Deposited 2008-06-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa） Fragment：UNP residues 45 to 522
Not recorded SO4 SULFATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 GSH Glutathione × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；298 K；3% ammonium sulfate, 0.1 M potassium phosphate and 0.1% beta-octyl glucoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00
Resolution 1.20 Å R-free 0.164
3DK8 Catalytic cycle of human glutathione reductase near 1 A resolution Deposited 2008-06-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa） Fragment：UNP residues 45 to 522
Not recorded SO4 SULFATE ION × 4 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 4 GOL GLYCEROL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；298 K；3% ammonium sulfate, 0.1 M potassium phosphate and 0.1% beta-octyl glucoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00
Resolution 1.10 Å R-free 0.157
3DK9 Catalytic cycle of human glutathione reductase near 1 A resolution Deposited 2008-06-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa） Fragment：UNP residues 45 to 522
Not recorded SO4 SULFATE ION × 6 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；298 K；3% ammonium sulfate, 0.1 M potassium phosphate and 0.1% beta-octyl glucoside, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 7.00
Resolution 0.95 Å R-free 0.152
3GRS REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION Deposited 1988-02-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.54 Å
3GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX Deposited 1997-02-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 18–478（461 aa）
Mutation：A34E, R37W FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 TS2 2-AMINO-4-[4-(4-AMINO-4-CARBOXY-BUTYRYLAMINO)-5,8,19,22-TETRAOXO-1,2-DITHIA-6,9,13,18,21-PENTAAZA-CYCLOTETRACOS-23-YLCARBAMOYL]-BUTYRIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；0.57-0.90 M AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION. CRYSTALS WERE SOAKED IN ARTIFICIAL MOTHER LIQUOR AT PH 6.5 CONTAINING 80 MM OXIDIZED TRYPANOTHIONE, vapor diffusion - hanging drop
Resolution 2.50 Å
3SQP Structure of human glutathione reductase complexed with pyocyanin, an agent with antimalarial activity Deposited 2011-07-06 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 45–522（478 aa）
Chain B 45–522（478 aa）
Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 4 3J8 5-methylphenazin-1(5H)-one × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；660 MM AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K
Resolution 2.21 Å R-free 0.182
4GR1 THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE Deposited 1990-03-26 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–478（478 aa）
Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 RGS 4N-MALONYL-CYSTEINYL-2,4-DIAMINOBUTYRATE DISULFIDE × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å
4GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME Deposited 1997-02-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 18–478（461 aa）
Mutation：A34E, R37W FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GCG BIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；0.57-0.90 M AMMONIUM SULFATE,100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION. CRYSTALS WERE SOAKED IN ARTIFICIAL MOTHER LIQUOR AT PH 6.5 CONTAINING 420 MM OXIDIZED GLUTATHIONE, vapor diffusion - hanging drop
Resolution 2.80 Å
5GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX Deposited 1997-02-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 18–478（461 aa）
Mutation：A34E, R37W FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 TS4 GLUTATHIONYLSPERMIDINE DISULFIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；0.57-0.90 M AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 8.0, AND 0.5% 1-N-BETA-OCTYL-D-GLUCOPYRANOSIDE HANGING DROP VAPOR DIFFUSION, CRYSTAL SOAKED IN ARTIFICIAL MOTHER LIQUOR AT PH 8.0,CONTAINING 0.5% BETA-OCTYL GLUCOSIDE AND 42 MM GLUTATHIONYLSPERMIDINE.
Resolution 2.40 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.