SAXSdb — 1cc4

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

PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE)

Pseudomonas fluorescens

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	蛋白单体单体蛋白 × 1 PDB 声明：monomeric（1）与蛋白拷贝数一致	链 A； UniProt 1–394	突变：F161A, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray结晶条件：pH 7；pH 7.0	分辨率 2.00 Å
2	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 1–394	突变：F161A, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件：pH 7；pH 7.0	分辨率 2.00 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 1CC4	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
1BF3 P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 42 REPLACED BY LYS (R42K), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID 提交 1998-05-26	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	突变：R42K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.20 Å
1BGJ P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND HIS 162 REPLACED BY ARG (H162R), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID 提交 1998-05-29	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	突变：C116S, H162R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 3.00 Å
1BGN P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 269 REPLACED BY THR (R269T), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID 提交 1998-05-29	突变/修饰不同实验环境不同	Assembly 1 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	突变：C116S, R269T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.00 Å
1BKW p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid 提交 1998-07-13	突变/修饰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 1–394（394 aa）	突变：R44K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.20 Å
1BKW p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid 提交 1998-07-13	突变/修饰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 1–394（394 aa）	突变：R44K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.20 Å
1CC6 PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY. 提交 1999-03-04	突变/修饰不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 1–394（394 aa）	突变：R166S, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray结晶条件 pH 7；pH 7.0	分辨率 2.20 Å
1CJ2 MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/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 × 2 PDB 声明：dimeric	链 A 1–391（391 aa）	突变：Q34R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.80 Å
1CJ2 MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/修饰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 1–391（391 aa）	突变：Q34R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.80 Å
1CJ3 MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/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 × 2 PDB 声明：dimeric	链 A 1–392（392 aa）	突变：Y38E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.50 Å
1CJ3 MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/修饰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 1–392（392 aa）	突变：Y38E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.50 Å
1CJ4 MUTANT Q34T OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/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 × 2 PDB 声明：dimeric	链 A 1–392（392 aa）	突变：Q34T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.40 Å
1CJ4 MUTANT Q34T OF PARA-HYDROXYBENZOATE HYDROXYLASE 提交 1999-04-21	构建体不同突变/修饰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 1–392（392 aa）	突变：Q34T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray结晶条件 pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	分辨率 2.40 Å
1PBB CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING 提交 1994-07-06	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DOB 2,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.50 Å
1PBC CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING 提交 1994-07-06	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 BHA 2-HYDROXY-4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.80 Å
1PBD CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING 提交 1994-07-06	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PAB 4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.30 Å
1PBE CRYSTAL STRUCTURE OF THE P-HYDROXYBENZOATE HYDROXYLASE-SUBSTRATE COMPLEX REFINED AT 1.9 ANGSTROMS RESOLUTION. ANALYSIS OF THE ENZYME-SUBSTRATE AND ENZYME-PRODUCT COMPLEXES 提交 1994-07-06	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 1.90 Å
1PBF CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING 提交 1994-07-06	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 BHA 2-HYDROXY-4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.70 Å
1PDH CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN 提交 1994-12-01	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 1–394（394 aa）	未记录	FAS ARABINO-FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.10 Å
1PHH CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE 提交 1987-11-04	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 1–394（394 aa）	未记录	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DHB 3,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.30 Å
2PHH THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE DISPLACES FAD IN THE ACTIVE SITE OF P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY CRYSTALLOGRAPHIC INVESTIGATION 提交 1989-06-19	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 × 2 PDB 声明：dimeric	链 A 1–394（394 aa）	未记录	APR ADENOSINE-5-DIPHOSPHORIBOSE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF 未提供已读取条件	分辨率 2.70 Å

共 16 个其他 PDB 条目、20 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	PHHY_PSEFL
Isoform	—
PDB实体	1
链与序列区间	作者链 A； PDB构建体 1–394； UniProt 1–394

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	1cc4
沉积日期 deposition_date	1999-03-04
结构标题 title	PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.
关键词 keywords	OXIDOREDUCTASE, HYDROXYBENZOATE; 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	22.58 Å
回转半径 Rg (电子) rg_electron	21.55 Å
零角强度 I(0) i0	34634700.00
分子量 molecular_weight	44764.0 kDa
排除体积 excluded_volume	55839 Å³
包络体积 envelope_volume	64912 Å³
水化壳体积 shell_volume	24855 Å³
包络直径 envelope_diameter	74.0 Å
壳层 Rg shell_rg	28.57 Å
包络 Rg envelope_rg	21.80 Å
形状 Rg shape_rg	21.56 Å
总 Rg total_rg	22.38 Å
总原子数 total_atoms	3155
残基数 n_residues	391
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	71.8 Å
Rg (实空间) rg_real	22.53 Å
Rg 误差 (实空间) rg_real_error	0.38 Å
I(0) (实空间) i0_real	3.4630e+07
I(0) 误差 (实空间) i0_real_error	4.5270e+05
Rg (倒空间) rg_reciprocal	22.54 Å
I(0) (倒空间) i0_reciprocal	34630000.0000
解质量估计 total_estimate	0.8963
解质量评级 solution_quality	GOOD a GOOD solution
P(r) 峰数 n_peaks	2
主峰位置 r_peak_primary	26.1 Å
偏度 Skewness skewness	0.317
峰度 Kurtosis kurtosis	-0.360
角度范围 angular_range	— – 0.3500 Å⁻¹
当前正则化参数 α current_alpha	0.0000
最高正则化参数 α highest_alpha	11310000.0000
实空间数据点数 n_real_points	67
GNOM 版本 gnom_version	4.1.3
质量判据 quality_criteria	AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.996

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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	PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE)
分子量 formula_weight	44288.4 kDa
EC 编号 ec_number	1.14.13.2
突变 mutation	F161A, C116S
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	3447

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGAHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

来源 Source

来源生物 organism	Pseudomonas fluorescens
NCBI 分类编号 ncbi_taxonomy_id	294
宿主生物 host_organism	Escherichia coli

实体 2 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

实体 3 Entity 3 non-polymer

描述 description	P-HYDROXYBENZOIC ACID
分子量 formula_weight	138.1 kDa
来源方法 src_method	syn
拷贝数 entity_count	1

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	292

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7. 折叠分类 (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

结构域编号 domain_id	d1cc4a1
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.3.1.2 — FAD-linked reductases, N-terminal domain

结构域编号 domain_id	d1cc4a2
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.16 — FAD-linked reductases, C-terminal domain
超家族 Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
家族 Family family	d.16.1.2 — PHBH-like

CATH v4.4 (2 domains)

结构域编号 domain_id	1cc4A01
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	1cc4A02
类 Class class	3 — Alpha Beta
架构 Architecture architecture	30 — 2-Layer Sandwich
拓扑 Topology topology	9 — D-Amino Acid Oxidase; Chain A, domain 2
同源超家族 H-superfamily homologous superfamily	10 — D-Amino Acid Oxidase, subunit A, domain 2

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8. 引用文献 (10)

Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.

Febs Lett. (1999)

PMID: 10025942 · DOI: 10.1016/S0014-5793(98)01726-8 PRIMARY

;Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin. ;

Protein Sci. (1994)

PMID: 7756982 · DOI: 10.1002/pro.5560031210

;Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring. ;

Biochemistry (1994)

PMID: 7520279 · DOI: 10.1021/bi00199a044

Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.

Proteins (1992)

PMID: 1409567 · DOI: 10.1002/prot.340140205

Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

Febs Lett. (1990)

PMID: 2269354 · DOI: 10.1016/0014-5793(90)80843-8

;Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes. ;

J.Mol.Biol. (1989)

PMID: 2553983 · DOI: 10.1016/0022-2836(89)90158-7

;The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation. ;

Biochemistry (1989)

PMID: 2819062 · DOI: 10.1021/bi00444a011

Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.

J.Mol.Biol. (1988)

PMID: 3351945 · DOI: 10.1016/0022-2836(88)90307-5

Crystal structure of p-hydroxybenzoate hydroxylase.

J.Mol.Biol. (1979)

PMID: 40036 · DOI: 10.1016/0022-2836(79)90301-2

Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

J.Biol.Chem. (1975)

PMID: 807574

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晶胞边长 a length_a	71.700 Å
晶胞边长 b length_b	146.300 Å
晶胞边长 c length_c	88.500 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	90.00 °
晶胞分子数 Z z_pdb	8

空间群 space_group	C 2 2 21
空间群编号 int_tables_number	20
晶系 crystal_system	—

分辨率 resolution	2.000 Å
最低分辨率 resolution_low	8.000 Å
R 因子 r_factor	—
R_work r_work	0.1790
R_free r_free	—

fit	/app/data/saxs_computation/cc/1cc4/1cc4.fit
pddf	/app/data/pr_computation/cc/1cc4/1cc4.pr.out
profile	/app/data/saxs_computation/cc/1cc4/1cc4.dat

PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.

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

PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE)

当前结构中的状态

数据库中的同蛋白其他状态

SAXS 散射曲线 SAXS Profile

P(r) 距离分布 P(r) Distribution

2. 结构基本信息 2. Structure Basics

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

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

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

晶胞参数 Unit Cell

对称性 Symmetry

精修参数 Refinement

衍射实验 Diffraction