+Open data
-Basic information
Entry | Database: PDB / ID: 2kjy | ||||||
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Title | MYPT1(658-714) | ||||||
Components | Protein phosphatase 1 regulatory subunit 12A | ||||||
Keywords | SIGNALING PROTEIN / MYPT1 / phosphorylation / protein phosphatase 1 / myosin phosphatase / Alternative splicing / ANK repeat / Cytoplasm / Phosphoprotein / Polymorphism | ||||||
Function / homology | Function and homology information regulation of myosin-light-chain-phosphatase activity / positive regulation of myosin-light-chain-phosphatase activity / phosphatase regulator activity / PTW/PP1 phosphatase complex / contractile muscle fiber / regulation of nucleocytoplasmic transport / negative regulation of catalytic activity / RHO GTPases Activate ROCKs / RHO GTPases activate CIT / enzyme inhibitor activity ...regulation of myosin-light-chain-phosphatase activity / positive regulation of myosin-light-chain-phosphatase activity / phosphatase regulator activity / PTW/PP1 phosphatase complex / contractile muscle fiber / regulation of nucleocytoplasmic transport / negative regulation of catalytic activity / RHO GTPases Activate ROCKs / RHO GTPases activate CIT / enzyme inhibitor activity / centrosome cycle / A band / RHO GTPases activate PAKs / regulation of cell adhesion / stress fiber / RHO GTPases activate PKNs / 14-3-3 protein binding / protein dephosphorylation / kinetochore / Z disc / Regulation of PLK1 Activity at G2/M Transition / actin cytoskeleton / cellular response to xenobiotic stimulus / mitotic cell cycle / focal adhesion / centrosome / nucleolus / protein kinase binding / signal transduction / positive regulation of transcription by RNA polymerase II / nucleoplasm / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | minimized average, model 1 | ||||||
Authors | Mori, S. / Iwaoka, R. / Eto, M. / Ohki, S. | ||||||
Citation | Journal: Proteins / Year: 2009 Title: Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1 Authors: Mori, S. / Iwaoka, R. / Eto, M. / Ohki, S.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kjy.cif.gz | 381.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kjy.ent.gz | 319.5 KB | Display | PDB format |
PDBx/mmJSON format | 2kjy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kj/2kjy ftp://data.pdbj.org/pub/pdb/validation_reports/kj/2kjy | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6964.675 Da / Num. of mol.: 1 / Fragment: UNP residues 658- 714 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPP1R12A, MBS, MYPT1 / Plasmid: pET / Production host: Escherichia coli (E. coli) / References: UniProt: O14974 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.6-1.0mM MYPT1(658-714)-1, 0.6-1.0mM [U-99% 15N] MYPT1(658-714)-2, 0.6-1.0mM [U-99% 13C; U-99% 15N] MYPT1(658-714)-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: KCl @100 / pH: 6.0 / Pressure: ambient / Temperature: 285 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 750 MHz |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |