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1alg

SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES

Method: SOLUTION NMR Dmax: 24.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

P11

synthetic construct

UniProt P00390

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 436–459 Fragment：INTERSUBUNIT-CONTACT HELIX No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3.1；283 K Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1ALG Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BWC STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE Deposited 1998-09-23 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
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

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSHR_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–24； UniProt 436–459

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1alg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1alg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1alg
Deposition date deposition_date1997-06-03
Structure title titleSOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES
Keywords keywordsHUMAN GLUTATHIONE REDUCTASE, PROTEIN-DIMERIZATION INHIBITOR, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier8.69 Å
Radius of gyration Rg (electron density) rg_electron8.74 Å
Forward intensity I(0) i09891930.00
Molecular weight molecular_weight24228.0 kDa
Excluded volume excluded_volume29914 ų
Envelope volume envelope_volume6816 ų
Hydration-shell volume shell_volume6244 ų
Envelope diameter envelope_diameter33.2 Å
Shell Rg shell_rg14.82 Å
Envelope Rg envelope_rg10.52 Å
Shape Rg shape_rg8.66 Å
Total Rg total_rg9.51 Å
Total atoms total_atoms3340
Residues n_residues240
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax24.8 Å
Rg (real space) rg_real8.62 Å
Rg uncertainty (real space) rg_real_error0.04 Å
I(0) (real space) i0_real9.6690e+06
I(0) uncertainty (real space) i0_real_error6.5740e+04
Rg (reciprocal space) rg_reciprocal8.82 Å
I(0) (reciprocal space) i0_reciprocal9892000.0000
Solution quality estimate total_estimate0.6459
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary7.8 Å
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.721
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha7.7630
Highest regularization parameter α highest_alpha2061.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 0.941; Sysdev: 0.000; Positv: 1.000; Valcen: 0.626; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1alga_
Class classj — Peptides
Fold Fold foldj.61 — Human glutathione reductase (HGR) inhibitor
Superfamily Superfamily superfamilyj.61.1 — Human glutathione reductase (HGR) inhibitor
Family Family familyj.61.1.1 — Human glutathione reductase (HGR) inhibitor
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8. Citations (1)

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9. Files and Curves (10)