3h66

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms

Method: X-RAY DIFFRACTION D_max: 91.8 Å Quality: GOOD

▼

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

Serine/threonine-protein phosphatase 5

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	蛋白单体单体蛋白 × 1 PDB 声明：monomeric（1）与蛋白拷贝数一致	链 A； UniProt 176–490	片段：Catalytic domain, residues 176-490	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray结晶条件：VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.59 Å R-free 0.291
2	蛋白单体单体蛋白 × 1 PDB 声明：monomeric（1）与蛋白拷贝数一致	链 B； UniProt 176–490	片段：Catalytic domain, residues 176-490	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray结晶条件：VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.59 Å R-free 0.291

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 3H66	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
1A17 TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5 提交 1997-12-23	构建体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 1 蛋白同源多聚体同源多聚体；蛋白 × 4 PDB 声明：tetrameric	链 A 16–181（166 aa）片段：PROTEIN INTERACTING DOMAIN	未记录	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray结晶条件 pH 7.5；1.8 M AMMONIUM SULFATE, 4% MPD, 100 MM HEPES PH 7.5, 2 MM DTT	分辨率 2.45 Å R-free 0.298
1A17 TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5 提交 1997-12-23	构建体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 16–181（166 aa）片段：PROTEIN INTERACTING DOMAIN	未记录	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray结晶条件 pH 7.5；1.8 M AMMONIUM SULFATE, 4% MPD, 100 MM HEPES PH 7.5, 2 MM DTT	分辨率 2.45 Å R-free 0.298
1S95 Structure of serine/threonine protein phosphatase 5 提交 2004-02-03	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 169–499（331 aa）片段：catalytic domain	未记录	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	分辨率 1.60 Å R-free 0.209
1S95 Structure of serine/threonine protein phosphatase 5 提交 2004-02-03	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 B 169–499（331 aa）片段：catalytic domain	未记录	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	分辨率 1.60 Å R-free 0.209
1S95 Structure of serine/threonine protein phosphatase 5 提交 2004-02-03	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 3 蛋白同源多聚体同源多聚体；蛋白 × 2 PDB 声明：dimeric	链 A 169–499（331 aa）片段：catalytic domain 链 B 169–499（331 aa）片段：catalytic domain	未记录	MN MANGANESE (II) ION × 4 PO4 PHOSPHATE ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	分辨率 1.60 Å R-free 0.209
1WAO PP5 structure 提交 2004-10-27	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 1 23–499（477 aa）	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 PEG 6K 10%	分辨率 2.90 Å R-free 0.290
1WAO PP5 structure 提交 2004-10-27	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 2 23–499（477 aa）	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 PEG 6K 10%	分辨率 2.90 Å R-free 0.290
1WAO PP5 structure 提交 2004-10-27	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 3 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 3 23–499（477 aa）	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 PEG 6K 10%	分辨率 2.90 Å R-free 0.290
1WAO PP5 structure 提交 2004-10-27	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 4 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 4 23–499（477 aa）	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 PEG 6K 10%	分辨率 2.90 Å R-free 0.290
2BUG Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide 提交 2005-06-13	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验方法不同实验环境不同结构质量不同	Assembly 1 蛋白异源复合物异源复合物；蛋白 × 2 PDB 声明：dimeric	链 A 19–147（129 aa）片段：TETRATRICOPEPTIDE DOMAIN, RESIDUES 19-147	突变：YES	未记录非水小分子	SOLUTION NMR NMR测量条件 pH 6；298 K；离子强度（mmCIF原始值）55；压力 1.0 NMR测量条件 pH 6；298 K；离子强度（mmCIF原始值）55；压力 1.0 NMR测量条件 pH 6；298 K；离子强度（mmCIF原始值）55；压力 1.0 NMR测量条件 pH 6；298 K；离子强度（mmCIF原始值）55；压力 1.0 NMR样品组成 50MM MES, 5MM DTT (PH6.0) 10%D2O, 90% H2O	分辨率未提供
3H60 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms 提交 2009-04-23	配体/离子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 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, MPD 40%, PEG MME 5000 20%, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.00 Å R-free 0.219
3H60 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms 提交 2009-04-23	配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 B 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, MPD 40%, PEG MME 5000 20%, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.00 Å R-free 0.219
3H61 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with norcantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子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 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HC, 40% MPD, 20% PEG MME 5000 , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.45 Å R-free 0.194
3H61 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with norcantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HC, 40% MPD, 20% PEG MME 5000 , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.45 Å R-free 0.194
3H62 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 C 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.40 Å R-free 0.204
3H62 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 B 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.40 Å R-free 0.204
3H63 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.30 Å R-free 0.191
3H63 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 C 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.30 Å R-free 0.191
3H64 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with endothall 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.90 Å R-free 0.237
3H64 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with endothall 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	MN MANGANESE (II) ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.90 Å R-free 0.237
3H67 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms complexed with cantharidic acid 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.65 Å R-free 0.231
3H67 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms complexed with cantharidic acid 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.65 Å R-free 0.231
3H68 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.50 Å R-free 0.232
3H68 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form) 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 NHC (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 1.50 Å R-free 0.232
3H69 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms complexed with endothall 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 1 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.10 Å R-free 0.227
3H69 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms complexed with endothall 提交 2009-04-23	配体/离子不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 176–490（315 aa）片段：Catalytic domain, residues 176-490	未记录	ZN ZINC ION × 2 ENL (1R,2S,3R,4S)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K	分辨率 2.10 Å R-free 0.227
4ZVZ Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid 提交 2015-05-18	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 4TF (1R,2S,3R,4S,5S)-5-(propoxymethyl)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	分辨率 2.00 Å R-free 0.235
4ZVZ Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid 提交 2015-05-18	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 B 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 4TF (1R,2S,3R,4S,5S)-5-(propoxymethyl)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	分辨率 2.00 Å R-free 0.235
4ZVZ Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid 提交 2015-05-18	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 3 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 C 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 4TF (1R,2S,3R,4S,5S)-5-(propoxymethyl)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1 NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	分辨率 2.00 Å R-free 0.235
4ZVZ Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid 提交 2015-05-18	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 4 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 4TF (1R,2S,3R,4S,5S)-5-(propoxymethyl)-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	分辨率 2.00 Å R-free 0.235
4ZX2 Co-crystal structures of PP5 in complex with 5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid 提交 2015-05-19	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 4TE (1S,2R,3S,4R,5S)-5-methyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	分辨率 1.23 Å R-free 0.175
5HPE Phosphatase domain of PP5 bound to a phosphomimetic Cdc37 substrate peptide 提交 2016-01-20	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 1 信息不足单体；蛋白 × 1 PDB 声明：monomeric	链 A 175–499（325 aa）	突变：S13E	MN MANGANESE (II) ION × 2 NCO COBALT HEXAMMINE(III) × 2	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION；277 K；18% PEG, 8% ethylene glycol, 0.1M Hepes pH 7.5, 20mM hexamine cobolt chloride	分辨率 2.27 Å R-free 0.236
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor 提交 2017-01-12	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 169–499（331 aa）	未记录	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	分辨率 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor 提交 2017-01-12	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 2 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 B 169–499（331 aa）	未记录	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	分辨率 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor 提交 2017-01-12	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 3 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 C 169–499（331 aa）	未记录	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	分辨率 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor 提交 2017-01-12	构建体不同配体/离子不同实验环境不同结构质量不同	Assembly 4 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 D 169–499（331 aa）	未记录	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	分辨率 1.96 Å R-free 0.246
5WG8 Structure of PP5C with LB-100; 7-oxabicyclo[2.2.1]heptane-2,3-dicarbonyl moiety modeled in the density 提交 2017-07-13	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 蛋白单体单体；蛋白 × 1 PDB 声明：monomeric	链 A 169–499（331 aa）片段：UNP residues 169-499	未记录	MN MANGANESE (II) ION × 2 LB1 (1S,2R,3S,4R)-3-(4-methylpiperazine-1-carbonyl)-7-oxabicyclo[2.2.1]heptane-2-carboxylic acid × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1	X-RAY DIFFRACTION X-ray结晶条件 VAPOR DIFFUSION, SITTING DROP；pH 8；289.15 K；10 mM Tris-HCl pH 8.0, 35% 2-methyl-2,4-pentanediol, and 10% polyethylene glycol methyl ether 5000	分辨率 1.65 Å R-free 0.196
7ZR5 CryoEM structure of HSP90-CDC37-BRAF(V600E)-PP5(closed) complex 提交 2022-05-03	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 蛋白异源复合物异源复合物；蛋白 × 5 PDB 声明：pentameric	链 P 17–499（483 aa）	未记录	ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM缓冲液 pH 7.5 cryo-EM玻璃化条件冷冻剂 ETHANE	分辨率 3.90 Å
7ZR6 CryoEM structure of HSP90-CDC37-BRAF(V600E)-PP5(open) complex 提交 2022-05-03	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 蛋白异源复合物异源复合物；蛋白 × 5 PDB 声明：pentameric	链 P 17–499（483 aa）	未记录	ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM缓冲液 pH 7.5 cryo-EM玻璃化条件冷冻剂 ETHANE	分辨率 4.20 Å
8GAE Hsp90 provides platform for CRaf dephosphorylation by PP5 提交 2023-02-22	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验方法不同实验环境不同结构质量不同	Assembly 1 蛋白异源复合物异源复合物；蛋白 × 5 PDB 声明：pentameric	链 E 1–499（499 aa）	突变：H304A	K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2	ELECTRON MICROSCOPY cryo-EM缓冲液 pH 7.5 cryo-EM玻璃化条件冷冻剂 ETHANE；3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE	分辨率 3.30 Å
8GFT Hsp90 provides platform for CRaf dephosphorylation by PP5 提交 2023-03-08	构建体不同突变/修饰不同聚集状态不同配体/离子不同实验方法不同实验环境不同结构质量不同	Assembly 1 蛋白异源复合物异源复合物；蛋白 × 5 PDB 声明：pentameric	链 E 1–499（499 aa）	突变：H304A	ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2	ELECTRON MICROSCOPY cryo-EM缓冲液 pH 7.5 cryo-EM玻璃化条件冷冻剂 ETHANE；3uL OF SAMPLE, 10C, 100% HUMIDITY, 30S WAIT TIME, 3S BLOT TIME, -2 BLOT FORCE	分辨率 3.80 Å

共 21 个其他 PDB 条目、41 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	PPP5_HUMAN
Isoform	—
PDB实体	1
链与序列区间	作者链 A； PDB构建体 1–315； UniProt 176–490 作者链 B； PDB构建体 1–315； UniProt 176–490

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

▼

2. 结构基本信息 2. Structure Basics

条目编号 entry_id	3h66
沉积日期 deposition_date	2009-04-23
结构标题 title	Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms
关键词 keywords	metalloenzyme, phosphatase, Cytoplasm, Hydrolase, Iron, Manganese, Metal-binding, Nucleus, Protein phosphatase, TPR repeat; HYDROLASE
实验方法 method	X-RAY DIFFRACTION

▼

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

回转半径 Rg (Guinier) rg_guinier	28.89 Å
回转半径 Rg (电子) rg_electron	28.46 Å
零角强度 I(0) i0	83416100.00
分子量 molecular_weight	72027.0 kDa
排除体积 excluded_volume	90025 Å³
包络体积 envelope_volume	106460 Å³
水化壳体积 shell_volume	31119 Å³
包络直径 envelope_diameter	96.8 Å
壳层 Rg shell_rg	35.81 Å
包络 Rg envelope_rg	28.37 Å
形状 Rg shape_rg	28.46 Å
总 Rg total_rg	29.18 Å
总原子数 total_atoms	5060
残基数 n_residues	630
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

▼

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

最大尺寸 Dmax dmax	91.8 Å
Rg (实空间) rg_real	28.92 Å
Rg 误差 (实空间) rg_real_error	0.77 Å
I(0) (实空间) i0_real	8.3420e+07
I(0) 误差 (实空间) i0_real_error	1.2340e+06
Rg (倒空间) rg_reciprocal	28.91 Å
I(0) (倒空间) i0_reciprocal	83420000.0000
解质量估计 total_estimate	0.8946
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	28.4 Å
偏度 Skewness skewness	0.323
峰度 Kurtosis kurtosis	-0.603
角度范围 angular_range	— – 0.2750 Å⁻¹
当前正则化参数 α current_alpha	0.0000
最高正则化参数 α highest_alpha	21540000.0000
实空间数据点数 n_real_points	56
GNOM 版本 gnom_version	4.1.3
质量判据 quality_criteria	AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.968

▶

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

▶

6. 实体与聚合物信息 Entities & Polymers (3)

实体 1 Entity 1 polymer

描述 description	Serine/threonine-protein phosphatase 5
分子量 formula_weight	35950.8 kDa
EC 编号 ec_number	3.1.3.16
来源方法 src_method	man
拷贝数 entity_count	2

聚合物 Polymer

聚合物类型 type	polypeptide(L)
链编号 strand_id	A,B
原子数 atom_count	5116

YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYA

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 BL21(DE3)

实体 2 Entity 2 non-polymer

描述 description	ZINC ION
分子量 formula_weight	65.4 kDa
来源方法 src_method	syn
拷贝数 entity_count	4

实体 3 Entity 3 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	56

▼

7. 折叠分类 (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

结构域编号 domain_id	d3h66a_
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.159 — Metallo-dependent phosphatases
超家族 Superfamily superfamily	d.159.1 — Metallo-dependent phosphatases
家族 Family family	d.159.1.3 — Protein serine/threonine phosphatase

结构域编号 domain_id	d3h66b_
类 Class class	d — Alpha and beta proteins (a+b)
折叠类型 Fold fold	d.159 — Metallo-dependent phosphatases
超家族 Superfamily superfamily	d.159.1 — Metallo-dependent phosphatases
家族 Family family	d.159.1.3 — Protein serine/threonine phosphatase

CATH v4.4 (2 domains)

结构域编号 domain_id	3h66A00
类 Class class	3 — Alpha Beta
架构 Architecture architecture	60 — 4-Layer Sandwich
拓扑 Topology topology	21 — Purple Acid Phosphatase; chain A, domain 2
同源超家族 H-superfamily homologous superfamily	10 — Metallo-dependent phosphatases

结构域编号 domain_id	3h66B00
类 Class class	3 — Alpha Beta
架构 Architecture architecture	60 — 4-Layer Sandwich
拓扑 Topology topology	21 — Purple Acid Phosphatase; chain A, domain 2
同源超家族 H-superfamily homologous superfamily	10 — Metallo-dependent phosphatases

▶

8. 引用文献 (1)

▶

晶胞边长 a length_a	154.251 Å
晶胞边长 b length_b	41.684 Å
晶胞边长 c length_c	106.092 Å
晶胞夹角 α angle_alpha	90.00 °
晶胞夹角 β angle_beta	96.46 °
晶胞夹角 γ angle_gamma	90.00 °
晶胞分子数 Z z_pdb	8

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	2.590 Å
最低分辨率 resolution_low	38.320 Å
R 因子 r_factor	0.2077
R_work r_work	0.1992
R_free r_free	0.2914

fit	/app/data/saxs_computation/h6/3h66/3h66.fit
pddf	/app/data/pr_computation/h6/3h66/3h66.pr.out
profile	/app/data/saxs_computation/h6/3h66/3h66.dat