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Yorodumi- PDB-2k3s: HADDOCK-derived structure of the CH-domain of the smoothelin-like... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2k3s | ||||||
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Title | HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin | ||||||
Components |
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Keywords | PROTEIN BINDING / apocalmodulin complex / calponin homology domain / smoothelin-like 1 / HADDOCK model / CH-domain / Coiled coil / Acetylation / Calcium / Methylation | ||||||
Function / homology | Function and homology information myosin phosphatase regulator activity / CH domain binding / muscle organ morphogenesis / contractile muscle fiber / protein phosphatase 1 binding / vasoconstriction / M band / I band / microtubule organizing center / protein phosphatase inhibitor activity ...myosin phosphatase regulator activity / CH domain binding / muscle organ morphogenesis / contractile muscle fiber / protein phosphatase 1 binding / vasoconstriction / M band / I band / microtubule organizing center / protein phosphatase inhibitor activity / tropomyosin binding / filamentous actin / enzyme regulator activity / positive regulation of vasoconstriction / response to activity / disordered domain specific binding / actin cytoskeleton organization / calmodulin binding / response to xenobiotic stimulus / signaling receptor binding / negative regulation of DNA-templated transcription / calcium ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Xenopus laevis (African clawed frog) | ||||||
Method | SOLUTION NMR / HADDOCK docking calculation | ||||||
Authors | Ishida, H. / Borman, M.A. / Ostrander, J. / Vogel, H.J. / MacDonald, J.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2008 Title: Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation. Authors: Ishida, H. / Borman, M.A. / Ostrander, J. / Vogel, H.J. / MacDonald, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k3s.cif.gz | 542.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k3s.ent.gz | 454.6 KB | Display | PDB format |
PDBx/mmJSON format | 2k3s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k3/2k3s ftp://data.pdbj.org/pub/pdb/validation_reports/k3/2k3s | HTTPS FTP |
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-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: 13693.794 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Smtnl1 / Plasmid: pGEX-6P1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q99LM3 |
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#2: Protein | Mass: 7737.468 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Gene: calm1 / Plasmid: Ptnco12 / Production host: Escherichia coli (E. coli) / References: UniProt: P62155, UniProt: P0DP33*PLUS |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D 1H-15N HSQC |
-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 7 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: HADDOCK docking calculation / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 15 |