SAXSdb — 1grt

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1. 结构基本信息 1. Structure Basics

条目编号 entry_id	1grt
沉积日期 deposition_date	1996-12-17
结构标题 title	HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT
关键词 keywords	OXIDOREDUCTASE (FLAVOENZYME); OXIDOREDUCTASE (FLAVOENZYME)
实验方法 method	X-RAY DIFFRACTION

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2. SAXS 参数 (CRYSOL 理论计算) 2. SAXS Parameters (CRYSOL)

回转半径 Rg (Guinier) rg_guinier	24.89 Å
回转半径 Rg (电子) rg_electron	23.96 Å
零角强度 I(0) i0	43534700.00
分子量 molecular_weight	50856.0 kDa
排除体积 excluded_volume	63648 Å³
包络体积 envelope_volume	77181 Å³
水化壳体积 shell_volume	26806 Å³
包络直径 envelope_diameter	78.0 Å
壳层 Rg shell_rg	31.17 Å
包络 Rg envelope_rg	23.96 Å
形状 Rg shape_rg	23.96 Å
总 Rg total_rg	24.79 Å
总原子数 total_atoms	3564
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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3. P(r) 距离分布 (GNOM 反演) 3. P(r) Analysis (GNOM)

最大尺寸 Dmax dmax	76.0 Å
Rg (实空间) rg_real	24.74 Å
Rg 误差 (实空间) rg_real_error	0.52 Å
I(0) (实空间) i0_real	4.3530e+07
I(0) 误差 (实空间) i0_real_error	5.8730e+05
Rg (倒空间) rg_reciprocal	24.77 Å
I(0) (倒空间) i0_reciprocal	43540000.0000
解质量估计 total_estimate	0.9138
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	32.6 Å
偏度 Skewness skewness	0.113
峰度 Kurtosis kurtosis	-0.596
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	7463000.0000
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: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.992

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4. 晶体学与实验 4. Crystallography & Experiment

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5. 实体与聚合体信息 (2)

Entity 1 polymer

描述 description	GLUTATHIONE REDUCTASE
分子量 formula_weight	51723.3 kDa
EC 编号 ec_number	1.6.4.2
突变 mutation	A34E, R37W
来源方法 src_method	man
拷贝数 entity_count	1

聚合体 Polymer

聚合体类型 type	polypeptide(L)
链编号 strand_id	A
原子数 atom_count	3564

ACRQEPQPQGPPPAAGAVASYDYLVIGGGSGGLESAWRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR

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

Entity 2 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

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6. 折叠分类 (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

结构域编号 domain_id	d1grta1
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	d1grta2
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	d1grta3
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	1grtA01
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	1grtA02
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	1grtA03
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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7. 引用文献 (13)

Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.

Biochemistry (1997)

PMID: 9174360 · DOI: 10.1021/bi963074p PRIMARY

Redox Enzyme Engineering: Conversion of Human Glutathione Reductase Into a Trypanothione Reductase

Biochemistry (1991)

Refined Structure of Glutathione Reductase at 1.54 A Resolution

J.Mol.Biol. (1987)

The Catalytic Mechanism of Glutathione Reductase as Derived from X-Ray Diffraction Analyses of Reaction Intermediates

J.Biol.Chem. (1983)

;Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase ;

J.Mol.Biol. (1983)

Glutathione Reductase from Human Erythrocytes. The Sequences of the Nadph Domain and of the Interface Domain

Eur.J.Biochem. (1982)

Fad-Binding Site of Glutathione Reductase

J.Mol.Biol. (1982)

Three-Dimensional Structure of Glutathione Reductase at 2 A Resolution

J.Mol.Biol. (1981)

Gene Duplication in Glutathione Reductase

J.Mol.Biol. (1980)

The C-Terminal Fragment of Human Glutathione Reductase Contains the Postulated Catalytic Histidine

FEBS Lett. (1979)

The Structure of the Flavoenzyme Glutathione Reductase

Nature (1978)

Low Resolution Structure of Human Erythrocyte Glutathione Reductase

J.Mol.Biol. (1977)

Crystals of Human Erythrocyte Glutathione Reductase

FEBS Lett. (1975)

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晶胞边长 a length_a	119.800 Å
晶胞边长 b length_b	84.500 Å
晶胞边长 c length_c	63.200 Å
晶胞夹角 α angle_alpha	90.00 °
晶胞夹角 β angle_beta	90.00 °
晶胞夹角 γ angle_gamma	58.70 °
晶胞分子数 Z z_pdb	4

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

分辨率 resolution	2.300 Å
最低分辨率 resolution_low	10.000 Å
R 因子 r_factor	0.2090
R_work r_work	0.2090
R_free r_free	—

fit	/app/data/saxs_computation/gr/1grt/1grt.fit
pddf	/app/data/pr_computation/gr/1grt/1grt.pr.out
profile	/app/data/saxs_computation/gr/1grt/1grt.dat

HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT

SAXS 散射曲线 SAXS Profile

P(r) 距离分布 P(r) Distribution

1. 结构基本信息 1. Structure Basics

2. SAXS 参数 (CRYSOL 理论计算) 2. SAXS Parameters (CRYSOL)

3. P(r) 距离分布 (GNOM 反演) 3. P(r) Analysis (GNOM)

4. 晶体学与实验 4. Crystallography & Experiment

晶胞参数 Unit Cell

对称性 Symmetry

精修参数 Refinement

衍射实验 Diffraction