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Yorodumi- PDB-2e73: Solution structure of the phorbol esters/diacylglycerol binding d... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2.0E+73 | ||||||
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Title | Solution structure of the phorbol esters/diacylglycerol binding domain of protein kinase C gamma | ||||||
Components | Protein kinase C gamma type | ||||||
Keywords | TRANSFERASE / C1 domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / regulation of response to food / calcium,diacylglycerol-dependent serine/threonine kinase activity / positive regulation of mismatch repair / Trafficking of GluR2-containing AMPA receptors / WNT5A-dependent internalization of FZD4 / chemosensory behavior / protein kinase C / negative regulation of proteasomal protein catabolic process ...Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / regulation of response to food / calcium,diacylglycerol-dependent serine/threonine kinase activity / positive regulation of mismatch repair / Trafficking of GluR2-containing AMPA receptors / WNT5A-dependent internalization of FZD4 / chemosensory behavior / protein kinase C / negative regulation of proteasomal protein catabolic process / diacylglycerol-dependent serine/threonine kinase activity / innervation / regulation of phagocytosis / response to morphine / presynaptic cytosol / Calmodulin induced events / postsynaptic cytosol / response to pain / response to psychosocial stress / regulation of synaptic vesicle exocytosis / calyx of Held / negative regulation of protein ubiquitination / presynaptic modulation of chemical synaptic transmission / protein serine/threonine/tyrosine kinase activity / synaptic membrane / long-term synaptic potentiation / regulation of circadian rhythm / negative regulation of protein catabolic process / response to toxic substance / G alpha (z) signalling events / rhythmic process / cell-cell junction / chemical synaptic transmission / negative regulation of neuron apoptotic process / postsynaptic density / learning or memory / protein kinase activity / intracellular signal transduction / phosphorylation / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / perinuclear region of cytoplasm / zinc ion binding / ATP binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Tanabe, W. / Suzuki, S. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the phorbol esters/diacylglycerol binding domain of protein kinase C gamma Authors: Tanabe, W. / Suzuki, S. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2e73.cif.gz | 462.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2e73.ent.gz | 399.6 KB | Display | PDB format |
PDBx/mmJSON format | 2e73.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e7/2e73 ftp://data.pdbj.org/pub/pdb/validation_reports/e7/2e73 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8678.886 Da / Num. of mol.: 1 / Fragment: C1 domain, residues 36-105 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: PRKCG, PKCG / Plasmid: P060626-05 / References: UniProt: P05129, protein kinase C |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O; 50uM Zncl2+1mM IDA; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |