1gd1

STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.8 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION D_max: 92.8 Å Quality: GOOD

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

HOLO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE

Geobacillus stearothermophilus

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 × 4 PDB 声明：tetrameric（4）与蛋白拷贝数一致	链 O； UniProt 1–334 链 P； UniProt 1–334 链 Q； UniProt 1–334 链 R； UniProt 1–334	未记录	SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION mmCIF 未提供已读取环境条件	分辨率 1.80 Å

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 1GD1	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
1DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+ 提交 1996-12-20	突变/修饰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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：D32G, L187A, P188S 突变：D32G, L187A, P188S 突变：D32G, L187A, P188S 突变：D32G, L187A, P188S	SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray结晶条件 pH 6.9；pH 6.9	分辨率 2.50 Å R-free 0.214
1NPT Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 replaced by Ala complexed with NAD+ 提交 2003-01-20	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：C149A 突变：C149A 突变：C149A 突变：C149A	SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.18 Å R-free 0.210
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ 提交 2003-01-21	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 Q 1–334（334 aa）	突变：C149S 突变：C149S	SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.11 Å R-free 0.249
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ 提交 2003-01-21	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–334（334 aa）链 C 1–334（334 aa）	突变：C149S 突变：C149S	SO4 SULFATE ION × 2 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.11 Å R-free 0.249
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ 提交 2003-01-21	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 3 蛋白同源多聚体同源多聚体；蛋白 × 4 PDB 声明：tetrameric	链 A 1–334（334 aa）链 C 1–334（334 aa）	突变：C149S 突变：C149S	SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.11 Å R-free 0.249
1NQA Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ala Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate 提交 2003-01-21	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：C149A 突变：C149A 突变：C149A 突变：C149A	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 4.6；293 K；PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.20 Å R-free 0.214
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate 提交 2003-01-22	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 Q 1–334（334 aa）	突变：C149S 突变：C149S	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.01 Å R-free 0.238
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate 提交 2003-01-22	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–334（334 aa）链 C 1–334（334 aa）	突变：C149S 突变：C149S	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.01 Å R-free 0.238
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate 提交 2003-01-22	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 3 蛋白同源多聚体同源多聚体；蛋白 × 4 PDB 声明：tetrameric	链 A 1–334（334 aa）链 C 1–334（334 aa）	突变：C149S 突变：C149S	NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 2.01 Å R-free 0.238
2DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+ 提交 1996-12-19	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：D32G, L187A, P188S 突变：D32G, L187A, P188S 突变：D32G, L187A, P188S 突变：D32G, L187A, P188S	SO4 SULFATE ION × 8 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray结晶条件 pH 6.9；pH 6.9	分辨率 2.20 Å R-free 0.265
2GD1 COENZYME-INDUCED CONFORMATIONAL CHANGES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILLUS 提交 1989-06-29	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	未记录	SO4 SULFATE ION × 8	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.50 Å
3CMC Thioacylenzyme intermediate of Bacillus stearothermophilus phosphorylating GAPDH 提交 2008-03-21	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 × 4 PDB 声明：tetrameric	链 O 2–335（334 aa）链 P 2–335（334 aa）链 Q 2–335（334 aa）链 R 2–335（334 aa）	未记录	SO4 SULFATE ION × 18 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 GOL GLYCEROL × 8 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 6.9；293 K；2.7 M Ammonium Sulfate, 100 mM Tris-HCl buffer pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K	分辨率 1.77 Å R-free 0.198
3DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+ 提交 1997-01-06	突变/修饰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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S	SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4	X-RAY DIFFRACTION X-ray结晶条件 pH 6.9；pH 6.9	分辨率 2.45 Å R-free 0.275
4DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+ 提交 1997-01-06	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 × 4 PDB 声明：tetrameric	链 O 1–334（334 aa）链 P 1–334（334 aa）链 Q 1–334（334 aa）链 R 1–334（334 aa）	突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S 突变：L33T, T34G, D36G, L187A, P188S	SO4 SULFATE ION × 8 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray结晶条件 pH 6.9；pH 6.9	分辨率 2.50 Å R-free 0.219

共 10 个其他 PDB 条目、14 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	G3P_BACST
Isoform	—
PDB实体	1
链与序列区间	作者链 O； PDB构建体 1–334； UniProt 1–334 作者链 P； PDB构建体 1–334； UniProt 1–334 作者链 Q； PDB构建体 1–334； UniProt 1–334 作者链 R； PDB构建体 1–334； UniProt 1–334

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。

SAXS 散射曲线 SAXS Profile

P(r) 距离分布 P(r) Distribution

下载 Download SAXS (.dat) P(r) (.pr.out) CIF

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2. 结构基本信息 2. Structure Basics

条目编号 entry_id	1gd1
沉积日期 deposition_date	1987-06-22
结构标题 title	STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.8 ANGSTROMS RESOLUTION
关键词 keywords	OXIDOREDUCTASE(ALDEHYDE(D)-NAD(A)); OXIDOREDUCTASE(ALDEHYDE(D)-NAD(A))
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	32.30 Å
回转半径 Rg (电子) rg_electron	31.72 Å
零角强度 I(0) i0	348734000.00
分子量 molecular_weight	147180.0 kDa
排除体积 excluded_volume	183210 Å³
包络体积 envelope_volume	217670 Å³
水化壳体积 shell_volume	54075 Å³
包络直径 envelope_diameter	98.6 Å
壳层 Rg shell_rg	41.11 Å
包络 Rg envelope_rg	31.77 Å
形状 Rg shape_rg	31.74 Å
总 Rg total_rg	32.34 Å
总原子数 total_atoms	10316
残基数 n_residues	1336
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	92.8 Å
Rg (实空间) rg_real	32.04 Å
Rg 误差 (实空间) rg_real_error	0.37 Å
I(0) (实空间) i0_real	3.4870e+08
I(0) 误差 (实空间) i0_real_error	4.1910e+06
Rg (倒空间) rg_reciprocal	32.15 Å
I(0) (倒空间) i0_reciprocal	348800000.0000
解质量估计 total_estimate	0.8971
解质量评级 solution_quality	GOOD a GOOD solution
P(r) 峰数 n_peaks	1
主峰位置 r_peak_primary	43.6 Å
偏度 Skewness skewness	0.075
峰度 Kurtosis kurtosis	-0.561
角度范围 angular_range	— – 0.2450 Å⁻¹
当前正则化参数 α current_alpha	0.0000
最高正则化参数 α highest_alpha	396000000.0000
实空间数据点数 n_real_points	50
GNOM 版本 gnom_version	4.1.3
质量判据 quality_criteria	AN1: 0.000; Oscil: 0.975; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.760

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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 (4)

实体 1 Entity 1 polymer

描述 description	HOLO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
分子量 formula_weight	35991.0 kDa
EC 编号 ec_number	1.2.1.12
来源方法 src_method	man
拷贝数 entity_count	4

聚合物 Polymer

聚合物类型 type	polypeptide(L)
链编号 strand_id	O,P,Q,R
原子数 atom_count	10984

AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDLPHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL

来源 Source

来源生物 organism	Geobacillus stearothermophilus
NCBI 分类编号 ncbi_taxonomy_id	1422

实体 2 Entity 2 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	8

实体 3 Entity 3 non-polymer

描述 description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
分子量 formula_weight	663.4 kDa
来源方法 src_method	syn
拷贝数 entity_count	4

实体 4 Entity 4 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	668

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7. 折叠分类 (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

结构域编号 domain_id	d1gd1o1
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
超家族 Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
家族 Family family	c.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain

结构域编号 domain_id	d1gd1o2
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.81 — FwdE/GAPDH domain-like
超家族 Superfamily superfamily	d.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
家族 Family family	d.81.1.1 — GAPDH-like

结构域编号 domain_id	d1gd1p1
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
超家族 Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
家族 Family family	c.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain

结构域编号 domain_id	d1gd1p2
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.81 — FwdE/GAPDH domain-like
超家族 Superfamily superfamily	d.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
家族 Family family	d.81.1.1 — GAPDH-like

结构域编号 domain_id	d1gd1q1
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
超家族 Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
家族 Family family	c.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain

结构域编号 domain_id	d1gd1q2
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.81 — FwdE/GAPDH domain-like
超家族 Superfamily superfamily	d.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
家族 Family family	d.81.1.1 — GAPDH-like

结构域编号 domain_id	d1gd1r1
类 Class class	c — Alpha and beta proteins (a/b)
折叠类型 Fold fold	c.2 — NAD(P)-binding Rossmann-fold domains
超家族 Superfamily superfamily	c.2.1 — NAD(P)-binding Rossmann-fold domains
家族 Family family	c.2.1.3 — Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain

结构域编号 domain_id	d1gd1r2
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.81 — FwdE/GAPDH domain-like
超家族 Superfamily superfamily	d.81.1 — Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain
家族 Family family	d.81.1.1 — GAPDH-like

CATH v4.4 (8 domains)

结构域编号 domain_id	1gd1O01
类 Class class	3 — Alpha Beta
架构 Architecture architecture	40 — 3-Layer(aba) Sandwich
拓扑 Topology topology	50 — Rossmann fold
同源超家族 H-superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

结构域编号 domain_id	1gd1O02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
同源超家族 H-superfamily homologous superfamily	10 — Dihydrodipicolinate Reductase; domain 2

结构域编号 domain_id	1gd1P01
类 Class class	3 — Alpha Beta
架构 Architecture architecture	40 — 3-Layer(aba) Sandwich
拓扑 Topology topology	50 — Rossmann fold
同源超家族 H-superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

结构域编号 domain_id	1gd1P02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
同源超家族 H-superfamily homologous superfamily	10 — Dihydrodipicolinate Reductase; domain 2

结构域编号 domain_id	1gd1Q01
类 Class class	3 — Alpha Beta
架构 Architecture architecture	40 — 3-Layer(aba) Sandwich
拓扑 Topology topology	50 — Rossmann fold
同源超家族 H-superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

结构域编号 domain_id	1gd1Q02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
同源超家族 H-superfamily homologous superfamily	10 — Dihydrodipicolinate Reductase; domain 2

结构域编号 domain_id	1gd1R01
类 Class class	3 — Alpha Beta
架构 Architecture architecture	40 — 3-Layer(aba) Sandwich
拓扑 Topology topology	50 — Rossmann fold
同源超家族 H-superfamily homologous superfamily	720 — NAD(P)-binding Rossmann-like Domain

结构域编号 domain_id	1gd1R02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	360 — Dihydrodipicolinate Reductase; domain 2
同源超家族 H-superfamily homologous superfamily	10 — Dihydrodipicolinate Reductase; domain 2

▶

8. 引用文献 (10)

Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution.

J.Mol.Biol. (1987)

PMID: 3586018 · DOI: 10.1016/0022-2836(87)90635-8 PRIMARY

;Nucleotide Sequence Determination of the DNA Region Coding for Bacillus Stearothermophilus Glyceraldehyde-3-Phosphate Dehydrogenase and of the Flanking DNA Regions Required for its Expression Escherichia Coli ;

Gene (1989)

Coenzyme-Induced Conformational Changes in Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus Stearothermophillus

J.Mol.Biol. (1988)

Structural Evidence for Ligand-Induced Sequential Conformational Changes in Glyceraldehyde 3-Phosphate Dehydrogenase

J.Mol.Biol. (1984)

Coenzyme Binding in Crystals of Glyceraldehyde-3-Phosphate Dehydrogenase

J.Mol.Biol. (1983)

Glyceraldehyde-3-Phosphate Dehydrogenase

Philos.Trans.R.Soc.London,Ser.B (1981)

Enzymes from Thermophilic Bacteria

Proc.FEBS Meet. (1978)

Sequence and Structure of D-Glyceraldehyde 3-Phosphate Dehydrogenase from Bacillus Stearothermophilus

Nature (1977)

Coenzyme Binding and Co-Operativity in D-Glyceraldehyde 3-Phosphate Dehydrogenase

Biochem.Soc.Trans. (1977)

Glyceraldehyde-3-Phosphate Dehydrogenase from Bacillus Stearothermophilus

FEBS Lett. (1971)

▶

晶胞边长 a length_a	82.440 Å
晶胞边长 b length_b	124.100 Å
晶胞边长 c length_c	82.540 Å
晶胞夹角 α angle_alpha	90.00 °
晶胞夹角 β angle_beta	108.98 °
晶胞夹角 γ angle_gamma	90.00 °
晶胞分子数 Z z_pdb	8

空间群 space_group	P 1 21 1
空间群编号 int_tables_number	4
晶系 crystal_system	—

分辨率 resolution	1.800 Å
最低分辨率 resolution_low	— Å
R 因子 r_factor	0.1770
R_work r_work	—
R_free r_free	—

fit	/app/data/saxs_computation/gd/1gd1/1gd1.fit
pddf	/app/data/pr_computation/gd/1gd1/1gd1.pr.out
profile	/app/data/saxs_computation/gd/1gd1/1gd1.dat