1s95

Structure of serine/threonine protein phosphatase 5

Method: X-RAY DIFFRACTION D_max: 89.5 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Serine/threonine protein phosphatase 5

Homo sapiens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 169–499	Fragment：catalytic domain	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.209
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 169–499	Fragment：catalytic domain	MN MANGANESE (II) ION × 2 PO4 PHOSPHATE ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.209
3	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 169–499 Chain B； UniProt 169–499	Fragment：catalytic domain	MN MANGANESE (II) ION × 4 PO4 PHOSPHATE ION × 2 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2-methyl,2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.60 Å R-free 0.209

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1S95	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1A17 TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5 Deposited 1997-12-23	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 16–181（166 aa） Fragment：PROTEIN INTERACTING DOMAIN	Not recorded	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.8 M AMMONIUM SULFATE, 4% MPD, 100 MM HEPES PH 7.5, 2 MM DTT	Resolution 2.45 Å R-free 0.298
1A17 TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5 Deposited 1997-12-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 16–181（166 aa） Fragment：PROTEIN INTERACTING DOMAIN	Not recorded	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；1.8 M AMMONIUM SULFATE, 4% MPD, 100 MM HEPES PH 7.5, 2 MM DTT	Resolution 2.45 Å R-free 0.298
1WAO PP5 structure Deposited 2004-10-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain 1 23–499（477 aa）	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions PEG 6K 10%	Resolution 2.90 Å R-free 0.290
1WAO PP5 structure Deposited 2004-10-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain 2 23–499（477 aa）	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions PEG 6K 10%	Resolution 2.90 Å R-free 0.290
1WAO PP5 structure Deposited 2004-10-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain 3 23–499（477 aa）	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions PEG 6K 10%	Resolution 2.90 Å R-free 0.290
1WAO PP5 structure Deposited 2004-10-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain 4 23–499（477 aa）	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions PEG 6K 10%	Resolution 2.90 Å R-free 0.290
2BUG Solution structure of the TPR domain from Protein phosphatase 5 in complex with Hsp90 derived peptide Deposited 2005-06-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 19–147（129 aa） Fragment：TETRATRICOPEPTIDE DOMAIN, RESIDUES 19-147	Mutation：YES	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 55；Pressure 1.0 NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 55；Pressure 1.0 NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 55；Pressure 1.0 NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 55；Pressure 1.0 NMR sample composition 50MM MES, 5MM DTT (PH6.0) 10%D2O, 90% H2O	Resolution not provided
3H60 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 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	Resolution 2.00 Å R-free 0.219
3H60 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Mn2+ atoms Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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 Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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 Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 1.30 Å R-free 0.191
3H64 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with endothall Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 1.90 Å R-free 0.237
3H64 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with endothall Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 1.90 Å R-free 0.237
3H66 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 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	Resolution 2.59 Å R-free 0.291
3H66 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions 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	Resolution 2.59 Å R-free 0.291
3H67 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms complexed with cantharidic acid Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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 Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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) Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 1.50 Å R-free 0.232
3H69 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms complexed with endothall Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 2.10 Å R-free 0.227
3H69 Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms complexed with endothall Deposited 2009-04-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 176–490（315 aa） Fragment：Catalytic domain, residues 176-490	Not recorded	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 crystallization conditions 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	Resolution 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 Deposited 2015-05-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	Resolution 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 Deposited 2015-05-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	Resolution 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 Deposited 2015-05-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	Resolution 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 Deposited 2015-05-18	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	Resolution 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 Deposited 2015-05-19	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；25% MPD, 6% PEG, 10 mM Tris, pH 8.0	Resolution 1.23 Å R-free 0.175
5HPE Phosphatase domain of PP5 bound to a phosphomimetic Cdc37 substrate peptide Deposited 2016-01-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 175–499（325 aa）	Mutation：S13E	MN MANGANESE (II) ION × 2 NCO COBALT HEXAMMINE(III) × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；277 K；18% PEG, 8% ethylene glycol, 0.1M Hepes pH 7.5, 20mM hexamine cobolt chloride	Resolution 2.27 Å R-free 0.236
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor Deposited 2017-01-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 169–499（331 aa）	Not recorded	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	Resolution 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor Deposited 2017-01-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 169–499（331 aa）	Not recorded	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	Resolution 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor Deposited 2017-01-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 169–499（331 aa）	Not recorded	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	Resolution 1.96 Å R-free 0.246
5UI1 Crystal Structure of Human Protein Phosphatase 5C (PP5C) in complex with a triazole inhibitor Deposited 2017-01-12	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain D 169–499（331 aa）	Not recorded	MN MANGANESE (II) ION × 2 8D4 5-phenyl-1H-1,2,3-triazole-4-carboxylic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；289 K；20-26% MPD, 4-8% PEG5000MME, 1 mM Manganese chloride, 10 mM Tris	Resolution 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 Deposited 2017-07-13	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 169–499（331 aa） Fragment：UNP residues 169-499	Not recorded	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 crystallization conditions 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	Resolution 1.65 Å R-free 0.196
7ZR5 CryoEM structure of HSP90-CDC37-BRAF(V600E)-PP5(closed) complex Deposited 2022-05-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain P 17–499（483 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
7ZR6 CryoEM structure of HSP90-CDC37-BRAF(V600E)-PP5(open) complex Deposited 2022-05-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain P 17–499（483 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.20 Å
8GAE Hsp90 provides platform for CRaf dephosphorylation by PP5 Deposited 2023-02-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–499（499 aa）	Mutation：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 buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE	Resolution 3.30 Å
8GFT Hsp90 provides platform for CRaf dephosphorylation by PP5 Deposited 2023-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–499（499 aa）	Mutation：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 buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3uL OF SAMPLE, 10C, 100% HUMIDITY, 30S WAIT TIME, 3S BLOT TIME, -2 BLOT FORCE	Resolution 3.80 Å

21 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PPP5_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–333； UniProt 169–499 Author chain B； PDBConstruct 3–333； UniProt 169–499

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

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

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1s95
Deposition date deposition_date	2004-02-03
Structure title title	Structure of serine/threonine protein phosphatase 5
Keywords keywords	protein phosphatase, PPPase, PP5, phosphate anion, metal ion, metallophosphoesterase, hydrolase; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	27.74 Å
Radius of gyration Rg (electron density) rg_electron	27.30 Å
Forward intensity I(0) i0	89802000.00
Molecular weight molecular_weight	74578.0 kDa
Excluded volume excluded_volume	93209 Å³
Envelope volume envelope_volume	108330 Å³
Hydration-shell volume shell_volume	32822 Å³
Envelope diameter envelope_diameter	95.0 Å
Shell Rg shell_rg	35.09 Å
Envelope Rg envelope_rg	27.56 Å
Shape Rg shape_rg	27.31 Å
Total Rg total_rg	28.03 Å
Total atoms total_atoms	5233
Residues n_residues	649
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	89.5 Å
Rg (real space) rg_real	27.75 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	8.9800e+07
I(0) uncertainty (real space) i0_real_error	1.3300e+06
Rg (reciprocal space) rg_reciprocal	27.75 Å
I(0) (reciprocal space) i0_reciprocal	89800000.0000
Solution quality estimate total_estimate	0.8936
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	28.3 Å
Skewness Skewness skewness	0.349
Kurtosis Kurtosis kurtosis	-0.512
Angular range angular_range	— – 0.2850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	34040000.0000
Real-space data points n_real_points	58
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.984

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Serine/threonine protein phosphatase 5
Molecular weight formula_weight	37887.0 kDa
EC 编号 ec_number	3.1.3.16
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5748

GASMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli BL21

Entity 2 Entity 2 non-polymer

Description description	MANGANESE (II) ION
Molecular weight formula_weight	54.9 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	(4S)-2-METHYL-2,4-PENTANEDIOL
Molecular weight formula_weight	118.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	463

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1s95a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamily	d.159.1 — Metallo-dependent phosphatases
Family Family family	d.159.1.3 — Protein serine/threonine phosphatase

Domain ID domain_id	d1s95b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamily	d.159.1 — Metallo-dependent phosphatases
Family Family family	d.159.1.3 — Protein serine/threonine phosphatase

CATH v4.4 (2 domains)

Domain ID domain_id	1s95A00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily	10 — Metallo-dependent phosphatases

Domain ID domain_id	1s95B00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily	10 — Metallo-dependent phosphatases

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8. Citations (1)

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Unit-cell length a length_a	40.808 Å
Unit-cell length b length_b	80.309 Å
Unit-cell length c length_c	92.189 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	94.25 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.600 Å
Low-resolution limit resolution_low	40.000 Å
R factor r_factor	0.1713
R_work r_work	0.1693
R_free r_free	0.2093

fit	/app/data/saxs_computation/s9/1s95/1s95.fit
pddf	/app/data/pr_computation/s9/1s95/1s95.pr.out
profile	/app/data/saxs_computation/s9/1s95/1s95.dat