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Yorodumi- PDB-2fcd: Solution structure of N-lobe Myosin Light Chain from Saccharomice... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fcd | ||||||
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Title | Solution structure of N-lobe Myosin Light Chain from Saccharomices cerevisiae | ||||||
Components | Myosin light chain 1 | ||||||
Keywords | CELL CYCLE / EF-HAND PROTEIN | ||||||
Function / homology | Function and homology information MIH complex / regulation of cell wall organization or biogenesis / regulation of actomyosin contractile ring contraction / RHO GTPases activate PAKs / protein localization to cell division site involved in mitotic actomyosin contractile ring assembly / myosin II heavy chain binding / cellular bud neck contractile ring / vesicle targeting / site of polarized growth / myosin V complex ...MIH complex / regulation of cell wall organization or biogenesis / regulation of actomyosin contractile ring contraction / RHO GTPases activate PAKs / protein localization to cell division site involved in mitotic actomyosin contractile ring assembly / myosin II heavy chain binding / cellular bud neck contractile ring / vesicle targeting / site of polarized growth / myosin V complex / mitotic actomyosin contractile ring assembly / cellular bud tip / septum digestion after cytokinesis / myosin V binding / cellular bud neck / vesicle transport along actin filament / myosin II complex / regulation of cytokinesis / vesicle / calcium ion binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Cicero, D.O. / Pennestri, M. / Contessa, G.M. / Paci, M. / Ragnini-Wilson, A. / Melino, S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: Structural basis for the interaction of the myosin light chain Mlc1p with the myosin V Myo2p IQ motifs. Authors: Pennestri, M. / Melino, S. / Contessa, G.M. / Casavola, E.C. / Paci, M. / Ragnini-Wilson, A. / Cicero, D.O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fcd.cif.gz | 34.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fcd.ent.gz | 24.9 KB | Display | PDB format |
PDBx/mmJSON format | 2fcd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2fcd_validation.pdf.gz | 240.7 KB | Display | wwPDB validaton report |
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Full document | 2fcd_full_validation.pdf.gz | 240.5 KB | Display | |
Data in XML | 2fcd_validation.xml.gz | 2.9 KB | Display | |
Data in CIF | 2fcd_validation.cif.gz | 3.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fc/2fcd ftp://data.pdbj.org/pub/pdb/validation_reports/fc/2fcd | 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: 8452.326 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: MLC1 / Production host: Escherichia coli (E. coli) / References: UniProt: P53141 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Details | Contents: 1 mM Mlc1p 15N, 13C; 50 mM phosphate buffer, Sodium Chloride 0.1 M; 90% H2O, 10% D2O Solvent system: 50 mM phosphate buffer, Sodium Chloride 0.1 M; 90% H2O, 10% D2O |
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Sample conditions | pH: 6.7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |