5y6o

Crystal structure of DAXX N-terminal four-helix bundle domain (4HB) in complex with ATRX

Method: X-RAY DIFFRACTION Dmax: 119.0 Å Quality: GOOD

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

Death domain-associated protein 6,Transcriptional regulator ATRX

Homo sapiens

UniProt P46100

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 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 A; UniProt 1265–1288 链 B; UniProt 1265–1288 链 C; UniProt 1265–1288 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297
2 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 D; UniProt 1265–1288 链 E; UniProt 1265–1288 链 F; UniProt 1265–1288 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297
3 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 G; UniProt 1265–1288 链 H; UniProt 1265–1288 链 I; UniProt 1265–1288 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297

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。

共 11 个其他 PDB 条目、16 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 ATRX_HUMAN
Isoform
PDB实体 1
链与序列区间 作者链 A; PDB构建体 96–119; UniProt 1265–1288 作者链 B; PDB构建体 96–119; UniProt 1265–1288 作者链 C; PDB构建体 96–119; UniProt 1265–1288 作者链 D; PDB构建体 96–119; UniProt 1265–1288 作者链 E; PDB构建体 96–119; UniProt 1265–1288 作者链 F; PDB构建体 96–119; UniProt 1265–1288 作者链 G; PDB构建体 96–119; UniProt 1265–1288 作者链 H; PDB构建体 96–119; UniProt 1265–1288 作者链 I; PDB构建体 96–119; UniProt 1265–1288

Death domain-associated protein 6,Transcriptional regulator ATRX

Homo sapiens

UniProt Q9UER7

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 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 A; UniProt 50–144 链 B; UniProt 50–144 链 C; UniProt 50–144 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297
2 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 D; UniProt 50–144 链 E; UniProt 50–144 链 F; UniProt 50–144 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297
3 信息不足 同源多聚体 蛋白 × 3 PDB 声明:trimeric(3) 与蛋白拷贝数一致 链 G; UniProt 50–144 链 H; UniProt 50–144 链 I; UniProt 50–144 片段:UNP residues 50-144,UNP residues 1265-1288 无其他共同聚合物 X-RAY DIFFRACTION X-ray结晶条件:VAPOR DIFFUSION, SITTING DROP;pH 6.8;293 K;The DAXX 4HB_ATRX DBM fusion protein at 26 mg/ml was crystallized under conditions of 0.1M Sodium Cacodylate, pH 6.8, 1.2 M Ammonium Sulfate and 3% 1, 5- Diaminopentane Dihydrochloride, using sitting-drop vapor-diffusion method at 293K. In this process, o.5 uL of protein was mixed with 0.5 uL of mother liquor. All the crystals were soaked in a cryoprotectant made from mother liquor supplemented with 25% glycerol before flash freezing in liquid nitrogen. 分辨率 3.10 Å R-free 0.297

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。

共 11 个其他 PDB 条目、16 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 DAXX_HUMAN
Isoform
PDB实体 1
链与序列区间 作者链 A; PDB构建体 1–95; UniProt 50–144 作者链 B; PDB构建体 1–95; UniProt 50–144 作者链 C; PDB构建体 1–95; UniProt 50–144 作者链 D; PDB构建体 1–95; UniProt 50–144 作者链 E; PDB构建体 1–95; UniProt 50–144 作者链 F; PDB构建体 1–95; UniProt 50–144 作者链 G; PDB构建体 1–95; UniProt 50–144 作者链 H; PDB构建体 1–95; UniProt 50–144 作者链 I; PDB构建体 1–95; UniProt 50–144

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

SAXS profile for 5y6o

P(r) 距离分布 P(r) Distribution

P(r) distribution for 5y6o
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2. 结构基本信息 2. Structure Basics

条目编号 entry_id5y6o
沉积日期 deposition_date2017-08-13
结构标题 titleCrystal structure of DAXX N-terminal four-helix bundle domain (4HB) in complex with ATRX
关键词 keywordsHistone chaperone, Gene repressor, GENE REGULATION; GENE REGULATION
实验方法 methodX-RAY DIFFRACTION

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

回转半径 Rg (Guinier) rg_guinier36.51
回转半径 Rg (电子) rg_electron36.04
零角强度 I(0) i0171107000.00
分子量 molecular_weight106320.0 kDa
排除体积 excluded_volume133910 ų
包络体积 envelope_volume193820 ų
水化壳体积 shell_volume46090 ų
包络直径 envelope_diameter126.8
壳层 Rg shell_rg41.44
包络 Rg envelope_rg35.02
形状 Rg shape_rg36.04
总 Rg total_rg36.50
总原子数 total_atoms7467
残基数 n_residues947
球谐函数阶数 n_harmonics20
q 范围 q_range— – 0.5000 −1
数据点数 n_points101
壳层类型 shell_typedirectional
溶剂电子密度 solvent_density0.3340 e/ų
壳层衬度 contrast_shell0.0300 e/ų
CRYSOL 版本 crysol_version4.1.3

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

最大尺寸 Dmax dmax119.0
Rg (实空间) rg_real36.50
Rg 误差 (实空间) rg_real_error1.07
I(0) (实空间) i0_real1.7110e+08
I(0) 误差 (实空间) i0_real_error2.7520e+06
Rg (倒空间) rg_reciprocal36.51
I(0) (倒空间) i0_reciprocal171100000.0000
解质量估计 total_estimate0.8929
解质量评级 solution_quality GOOD a GOOD solution
P(r) 峰数 n_peaks2
主峰位置 r_peak_primary41.5
偏度 Skewness skewness0.299
峰度 Kurtosis kurtosis-0.509
角度范围 angular_range— – 0.2150 −1
当前正则化参数 α current_alpha0.0000
最高正则化参数 α highest_alpha15970000.0000
实空间数据点数 n_real_points44
GNOM 版本 gnom_version4.1.3
质量判据 quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.900

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

6. 实体与聚合物信息 Entities & Polymers (1)

8. 引用文献 (1)

9. 文件与曲线 (10)