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Yorodumi- PDB-1z87: solution structure of the split PH-PDZ Supramodule of alpha-Syntrophin -
+Open data
-Basic information
Entry | Database: PDB / ID: 1z87 | ||||||
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Title | solution structure of the split PH-PDZ Supramodule of alpha-Syntrophin | ||||||
Components | Alpha-1-syntrophin | ||||||
Keywords | PROTEIN BINDING / Alpha-1-syntrophin | ||||||
Function / homology | Function and homology information regulation of vasoconstriction by circulating norepinephrine / negative regulation of peptidyl-cysteine S-nitrosylation / dystrophin-associated glycoprotein complex / regulation of sodium ion transmembrane transport / ventricular cardiac muscle cell action potential / regulation of ventricular cardiac muscle cell membrane repolarization / anchoring junction / neuromuscular junction development / nitric-oxide synthase binding / sodium channel regulator activity ...regulation of vasoconstriction by circulating norepinephrine / negative regulation of peptidyl-cysteine S-nitrosylation / dystrophin-associated glycoprotein complex / regulation of sodium ion transmembrane transport / ventricular cardiac muscle cell action potential / regulation of ventricular cardiac muscle cell membrane repolarization / anchoring junction / neuromuscular junction development / nitric-oxide synthase binding / sodium channel regulator activity / regulation of heart rate / PDZ domain binding / neuromuscular junction / sarcolemma / actin binding / ATPase binding / postsynaptic membrane / transmembrane transporter binding / cytoskeleton / calmodulin binding / structural molecule activity / protein-containing complex / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Yan, J. / Xu, W. / Wen, W. / Long, J.F. / Adams, M.E. / Froehner, S.C. / Zhang, M. | ||||||
Citation | Journal: Embo J. / Year: 2005 Title: Structure of the split PH domain and distinct lipid-binding properties of the PH-PDZ supramodule of alpha-syntrophin Authors: Yan, J. / Wen, W. / Xu, W. / Long, J.F. / Adams, M.E. / Froehner, S.C. / Zhang, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z87.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1z87.ent.gz | 954.6 KB | Display | PDB format |
PDBx/mmJSON format | 1z87.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z87_validation.pdf.gz | 347.8 KB | Display | wwPDB validaton report |
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Full document | 1z87_full_validation.pdf.gz | 529.5 KB | Display | |
Data in XML | 1z87_validation.xml.gz | 85.4 KB | Display | |
Data in CIF | 1z87_validation.cif.gz | 108.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z8/1z87 ftp://data.pdbj.org/pub/pdb/validation_reports/z8/1z87 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 27716.318 Da / Num. of mol.: 1 / Fragment: the PHN-PDZ-PHC tandem Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pET32a(modified version) / Production host: Escherichia coli (E. coli) / References: UniProt: Q61234 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | pH: 7.0 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 750 MHz |
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-Processing
NMR software | Name: CNS / Version: 1.1 / Developer: Bruger, A.T. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 2924 restraints, 2600 are NOE-derived distance constraints, 184 dihedral angle restraints,140 distance restraints from hydrogen bonds. this ensemble ...Details: the structures are based on a total of 2924 restraints, 2600 are NOE-derived distance constraints, 184 dihedral angle restraints,140 distance restraints from hydrogen bonds. this ensemble structure could not be superimposed because this protein fragment is a PH-PDZ tandem, and the linker is very flexible. |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 15 |