SAXSdb — 3djj

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1. 蛋白身份与相关结构 Protein Identity & Related Structures

Glutathione reductase, mitochondrial precursor

Homo sapiens

当前结构中的状态

Assembly	聚集状态	构建体	突变与修饰	配体、离子与共同组分	实验方法与环境	结构质量
1	蛋白同源多聚体同源多聚体蛋白 × 2 PDB 声明：dimeric（2）与蛋白拷贝数一致	链 A； UniProt 45–522	片段：UNP residues 45 to 522	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结晶条件：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	分辨率 1.10 Å R-free 0.147

数据库中的同蛋白其他状态

以下每一行都是同一 UniProt 蛋白在另一个 PDB 条目中的 biological assembly， “相对当前条目”直接指出证据层面的不同；没有差异标签表示当前已读取字段一致。

其他 PDB	相对当前条目 3DJJ	Assembly / 聚集状态	构建体	突变与修饰	配体、离子与非聚合物	实验方法与环境	结构质量
1ALG SOLUTION STRUCTURE OF AN HGR INHIBITOR, NMR, 10 STRUCTURES 提交 1997-06-03	构建体不同聚集状态不同配体/离子不同实验方法不同实验环境不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 436–459（24 aa）片段：INTERSUBUNIT-CONTACT HELIX	未记录	未记录非水小分子	SOLUTION NMR NMR测量条件 pH 3.1；283 K	分辨率未提供
1BWC STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE 提交 1998-09-23	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	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结晶条件 pH 6.9；pH 6.9	分辨率 2.10 Å R-free 0.230
1DNC HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON 提交 1998-02-20	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	非标准单体：是（mmCIF未提供具体位点）	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 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 提交 1992-12-15	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 GSH Glutathione × 4	X-RAY DIFFRACTION X-ray结晶条件 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.	分辨率 2.00 Å
1GRB SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION 提交 1992-12-15	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	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 未提供已读取条件	分辨率 1.85 Å
1GRE SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION 提交 1992-12-15	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 4	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.00 Å
1GRF SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION 提交 1992-12-15	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 ACM ACETAMIDE × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.00 Å
1GRG SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION 提交 1992-12-15	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	非标准单体：是（mmCIF未提供具体位点）	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 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 提交 1992-12-15	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 EOH ETHANOL × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 3.00 Å
1GRT HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT 提交 1996-12-17	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	突变：A34E, R37W	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.30 Å
1GSN HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE 提交 1998-02-21	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）	非标准单体：是（mmCIF未提供具体位点）	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.70 Å R-free 0.249
1K4Q Human Glutathione Reductase Inactivated by Peroxynitrite 提交 2001-10-08	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 62–522（461 aa）	非标准单体：是（mmCIF未提供具体位点）	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；Ammonium Sulfate, Potassium Phosphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 1.90 Å R-free 0.204
1XAN HUMAN GLUTATHIONE REDUCTASE IN COMPLEX WITH A XANTHENE INHIBITOR 提交 1996-01-26	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 18–478（461 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 HXP 3,6-DIHYDROXY-XANTHENE-9-PROPIONIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.00 Å
2AAQ Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI 提交 2005-07-14	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 44–522（479 aa）	未记录	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结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	分辨率 2.60 Å R-free 0.259
2GH5 Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5 提交 2006-03-25	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）片段：glutathione reductase 链 B 45–522（478 aa）片段：glutathione reductase	未记录	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结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100 mM potassium phosphate, pH 8.0 and 16% NH4SO4, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 1.70 Å R-free 0.256
2GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX 提交 1997-02-12	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 18–478（461 aa）	突变：A34E, R37W	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GDS OXIDIZED GLUTATHIONE DISULFIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.70 Å
3DJG Catalytic cycle of human glutathione reductase near 1 A resolution 提交 2008-06-23	构建体不同配体/离子不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 X 62–522（461 aa）片段：UNP residues 45 to 522	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.80 Å R-free 0.186
3DK4 Catalytic cycle of human glutathione reductase near 1 A resolution 提交 2008-06-24	配体/离子不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）片段：UNP residues 45 to 522	未记录	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结晶条件 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	分辨率 1.20 Å R-free 0.164
3DK8 Catalytic cycle of human glutathione reductase near 1 A resolution 提交 2008-06-24	配体/离子不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）片段：UNP residues 45 to 522	未记录	SO4 SULFATE ION × 4 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GSH Glutathione × 4 GOL GLYCEROL × 8	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 1.10 Å R-free 0.157
3DK9 Catalytic cycle of human glutathione reductase near 1 A resolution 提交 2008-06-24	配体/离子不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）片段：UNP residues 45 to 522	未记录	SO4 SULFATE ION × 6 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 0.95 Å R-free 0.152
3GRS REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION 提交 1988-02-05	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.54 Å
3GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX 提交 1997-02-12	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 18–478（461 aa）	突变：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结晶条件 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	分辨率 2.50 Å
3SQP Structure of human glutathione reductase complexed with pyocyanin, an agent with antimalarial activity 提交 2011-07-06	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 45–522（478 aa）链 B 45–522（478 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 SO4 SULFATE ION × 4 3J8 5-methylphenazin-1(5H)-one × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7.5；660 MM AMMONIUM SULFATE, 100 MM POTASSIUM PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K	分辨率 2.21 Å R-free 0.182
4GR1 THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE 提交 1990-03-26	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–478（478 aa）	未记录	PO4 PHOSPHATE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 RGS 4N-MALONYL-CYSTEINYL-2,4-DIAMINOBUTYRATE DISULFIDE × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.40 Å
4GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME 提交 1997-02-12	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 18–478（461 aa）	突变：A34E, R37W	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 GCG BIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE × 2	X-RAY DIFFRACTION X-ray结晶条件 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	分辨率 2.80 Å
5GRT HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX 提交 1997-02-12	构建体不同突变/修饰不同配体/离子不同实验环境不同结构质量不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 18–478（461 aa）	突变：A34E, R37W	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 TS4 GLUTATHIONYLSPERMIDINE DISULFIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 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.	分辨率 2.40 Å

共 26 个其他 PDB 条目、26 个 assembly。打开独立比较页并筛选聚集状态

查看构建体与数据证据

UniProt名称	GSHR_HUMAN
Isoform	—
PDB实体	1
链与序列区间	作者链 A； PDB构建体 1–478； UniProt 45–522

页面优先展示蛋白身份、当前 assembly、共同组分、聚集状态和跨 PDB 结构链接。链映射与序列区间收在“数据证据”中；数据库内部编号、导入时间和 assembly 操作表达式仅用于维护，因此不在读者页面展示。

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2. 结构基本信息 2. Structure Basics

条目编号 entry_id	3djj
沉积日期 deposition_date	2008-06-23
结构标题 title	Catalytic cycle of human glutathione reductase near 1 A resolution
关键词 keywords	;flavoenzyme, glutathione, nicotinamide, Alternative initiation, FAD, Flavoprotein, Mitochondrion, NADP, Oxidoreductase, Phosphoprotein, Redox-active center, Transit peptide ;; OXIDOREDUCTASE
实验方法 method	X-RAY DIFFRACTION

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3. SAXS 参数 (CRYSOL 理论计算) 3. SAXS Parameters (CRYSOL)

回转半径 Rg (Guinier) rg_guinier	24.64 Å
回转半径 Rg (电子) rg_electron	23.84 Å
零角强度 I(0) i0	49505500.00
分子量 molecular_weight	52673.0 kDa
排除体积 excluded_volume	65211 Å³
包络体积 envelope_volume	79479 Å³
水化壳体积 shell_volume	27510 Å³
包络直径 envelope_diameter	78.3 Å
壳层 Rg shell_rg	31.27 Å
包络 Rg envelope_rg	24.02 Å
形状 Rg shape_rg	23.86 Å
总 Rg total_rg	24.61 Å
总原子数 total_atoms	3674
残基数 n_residues	462
球谐函数阶数 n_harmonics	20
q 范围 q_range	— – 0.5000 Å⁻¹
数据点数 n_points	101
壳层类型 shell_type	directional
溶剂电子密度 solvent_density	0.3340 e/Å³
壳层衬度 contrast_shell	0.0300 e/Å³
CRYSOL 版本 crysol_version	4.1.3

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4. P(r) 距离分布 (GNOM 反演) 4. P(r) Analysis (GNOM)

最大尺寸 Dmax dmax	75.7 Å
Rg (实空间) rg_real	24.51 Å
Rg 误差 (实空间) rg_real_error	0.42 Å
I(0) (实空间) i0_real	4.9510e+07
I(0) 误差 (实空间) i0_real_error	6.3360e+05
Rg (倒空间) rg_reciprocal	24.54 Å
I(0) (倒空间) i0_reciprocal	49510000.0000
解质量估计 total_estimate	0.9115
解质量评级 solution_quality	EXCELLENT a EXCELLENT solution
P(r) 峰数 n_peaks	2
主峰位置 r_peak_primary	31.2 Å
偏度 Skewness skewness	0.151
峰度 Kurtosis kurtosis	-0.551
角度范围 angular_range	— – 0.3200 Å⁻¹
当前正则化参数 α current_alpha	0.0000
最高正则化参数 α highest_alpha	12270000.0000
实空间数据点数 n_real_points	64
GNOM 版本 gnom_version	4.1.3
质量判据 quality_criteria	AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.994

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5. 晶体学与实验 5. Crystallography & Experiment

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6. 实体与聚合物信息 Entities & Polymers (7)

实体 1 Entity 1 polymer

描述 description	Glutathione reductase, mitochondrial precursor
分子量 formula_weight	51636.2 kDa
EC 编号 ec_number	1.8.1.7
来源方法 src_method	man
拷贝数 entity_count	1

聚合物 Polymer

聚合物类型 type	polypeptide(L)
链编号 strand_id	A
原子数 atom_count	4923

ACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI 分类编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

实体 2 Entity 2 non-polymer

描述 description	PHOSPHATE ION
分子量 formula_weight	95.0 kDa
来源方法 src_method	syn
拷贝数 entity_count	5

实体 3 Entity 3 non-polymer

描述 description	SULFATE ION
分子量 formula_weight	96.1 kDa
来源方法 src_method	syn
拷贝数 entity_count	4

实体 4 Entity 4 non-polymer

描述 description	FLAVIN-ADENINE DINUCLEOTIDE
分子量 formula_weight	785.5 kDa
来源方法 src_method	syn
拷贝数 entity_count	1

实体 5 Entity 5 non-polymer

描述 description	NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
分子量 formula_weight	745.4 kDa
来源方法 src_method	syn
拷贝数 entity_count	1

实体 6 Entity 6 non-polymer

描述 description	GLYCEROL
分子量 formula_weight	92.1 kDa
来源方法 src_method	syn
拷贝数 entity_count	8

实体 7 Entity 7 water

描述 description	water
分子量 formula_weight	18.0 kDa
来源方法 src_method	nat
拷贝数 entity_count	878

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7. 折叠分类 (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

结构域编号 domain_id	d3djja1
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.3 — FAD/NAD(P)-binding domain
超家族 Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
家族 Family family	c.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains

结构域编号 domain_id	d3djja2
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.3 — FAD/NAD(P)-binding domain
超家族 Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
家族 Family family	c.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains

结构域编号 domain_id	d3djja3
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.87 — CO dehydrogenase flavoprotein C-domain-like
超家族 Superfamily superfamily	d.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
家族 Family family	d.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain

CATH v4.4 (3 domains)

结构域编号 domain_id	3djjA01
类 Class class	3 — Alpha Beta
架构 Architecture architecture	50 — 3-Layer(bba) Sandwich
拓扑 Topology topology	50 — FAD/NAD(P)-binding domain
同源超家族 H-superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

结构域编号 domain_id	3djjA02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	50 — 3-Layer(bba) Sandwich
拓扑 Topology topology	50 — FAD/NAD(P)-binding domain
同源超家族 H-superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

结构域编号 domain_id	3djjA03
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	390 — Enolase-like; domain 1
同源超家族 H-superfamily homologous superfamily	30 — FAD/NAD-linked reductase, C-terminal dimerisation domain

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8. 引用文献 (1)

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晶胞边长 a length_a	119.672 Å
晶胞边长 b length_b	62.358 Å
晶胞边长 c length_c	84.161 Å
晶胞夹角 α angle_alpha	90.00 °
晶胞夹角 β angle_beta	122.29 °
晶胞夹角 γ angle_gamma	90.00 °
晶胞分子数 Z z_pdb	4

空间群 space_group	C 1 2 1
空间群编号 int_tables_number	5
晶系 crystal_system	—

分辨率 resolution	1.100 Å
最低分辨率 resolution_low	100.000 Å
R 因子 r_factor	0.1130
R_work r_work	—
R_free r_free	0.1470

fit	/app/data/saxs_computation/dj/3djj/3djj.fit
pddf	/app/data/pr_computation/dj/3djj/3djj.pr.out
profile	/app/data/saxs_computation/dj/3djj/3djj.dat

Catalytic cycle of human glutathione reductase near 1 A resolution