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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

Method: X-RAY DIFFRACTION Dmax: 75.5 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GLUTATHIONE REDUCTASE

HOMO SAPIENS

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–478 Not recorded PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EOH ETHANOL × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å

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 1GRH Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ALG SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES Deposited 1997-06-03 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
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 Different ligand/ion 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 mutation/modification Different ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 mutation/modification Different ligand/ion 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
1GRT HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT Deposited 1996-12-17 Different mutation/modification Different ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 ligand/ion 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 1–478； UniProt 1–478

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 1grh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1grh
Deposition date deposition_date1992-12-15
Structure title titleINHIBITION OF HUMAN GLUTATHIONE REDUCTASE BY THE NITROSOUREA DRUGS 1,3-BIS(2-CHLOROETHYL)-1-NITROSOUREA AND 1-(2-CHLOROETHYL)-3-(2-HYDROXYETHYL)-1-NITROSOUREA
Keywords keywordsOXIDOREDUCTASE, FLAVOENZYME; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.92 Å
Radius of gyration Rg (electron density) rg_electron23.98 Å
Forward intensity I(0) i043964000.00
Molecular weight molecular_weight50840.0 kDa
Excluded volume excluded_volume63557 ų
Envelope volume envelope_volume78523 ų
Hydration-shell volume shell_volume27102 ų
Envelope diameter envelope_diameter78.1 Å
Shell Rg shell_rg31.33 Å
Envelope Rg envelope_rg24.06 Å
Shape Rg shape_rg23.99 Å
Total Rg total_rg24.82 Å
Total atoms total_atoms3560
Residues n_residues461
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 dmax75.5 Å
Rg (real space) rg_real24.77 Å
Rg uncertainty (real space) rg_real_error0.48 Å
I(0) (real space) i0_real4.3960e+07
I(0) uncertainty (real space) i0_real_error5.7170e+05
Rg (reciprocal space) rg_reciprocal24.81 Å
I(0) (reciprocal space) i0_reciprocal43970000.0000
Solution quality estimate total_estimate0.9133
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4 Å
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.593
Angular range angular_range— – 0.3200 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8481000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.983
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1grha_
Class classi — Low resolution protein structures
Fold Fold foldi.12 — Proteins of incorrect, partial and unknown sequence
Superfamily Superfamily superfamilyi.12.1 — Proteins of incorrect, partial and unknown sequence
Family Family familyi.12.1.1 — Proteins of incorrect, partial and unknown sequence

CATH v4.4 (3 domains)

Domain ID domain_id1grhA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1grhA02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1grhA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily30 — FAD/NAD-linked reductase, C-terminal dimerisation domain
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8. Citations (1)

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9. Files and Curves (10)