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- PDB-1tbn: NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MIN... -
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Basic information
Entry | Database: PDB / ID: 1tbn | ||||||
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Title | NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, MINIMIZED AVERAGE STRUCTURE | ||||||
![]() | PROTEIN KINASE C, GAMMA TYPE | ||||||
![]() | CALCIUM-BINDING PROTEIN / PROTEIN KINASE C / PKC / TRANSFERASE | ||||||
Function / homology | ![]() Calmodulin induced events / Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / regulation of response to food / positive regulation of mismatch repair / WNT5A-dependent internalization of FZD4 / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / calcium,diacylglycerol-dependent serine/threonine kinase activity / protein kinase C / diacylglycerol-dependent serine/threonine kinase activity ...Calmodulin induced events / Disinhibition of SNARE formation / Response to elevated platelet cytosolic Ca2+ / regulation of response to food / positive regulation of mismatch repair / WNT5A-dependent internalization of FZD4 / diacylglycerol-dependent, calcium-independent serine/threonine kinase activity / calcium,diacylglycerol-dependent serine/threonine kinase activity / protein kinase C / diacylglycerol-dependent serine/threonine kinase activity / negative regulation of proteasomal protein catabolic process / chemosensory behavior / innervation / regulation of phagocytosis / response to angiotensin / response to morphine / regulation of synaptic vesicle exocytosis / response to pain / phosphorylation / response to psychosocial stress / Trafficking of GluR2-containing AMPA receptors / postsynaptic cytosol / presynaptic cytosol / calyx of Held / negative regulation of protein ubiquitination / presynaptic modulation of chemical synaptic transmission / protein serine/threonine/tyrosine kinase activity / long-term synaptic potentiation / synaptic membrane / regulation of circadian rhythm / negative regulation of protein catabolic process / response to toxic substance / rhythmic process / cell-cell junction / presynapse / peptidyl-serine phosphorylation / protein autophosphorylation / chemical synaptic transmission / negative regulation of neuron apoptotic process / learning or memory / protein kinase activity / intracellular signal transduction / postsynaptic density / neuron projection / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / perinuclear region of cytoplasm / zinc ion binding / ATP binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / DG-SA | ||||||
![]() | Xu, R.X. / Pawelczyk, T. / Xia, T. / Brown, S.C. | ||||||
![]() | ![]() Title: NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions. Authors: Xu, R.X. / Pawelczyk, T. / Xia, T.H. / Brown, S.C. #1: ![]() Title: Crystal Structure of the Cys2 Activator-Binding Domain of Protein Kinase C Delta in Complex with Phorbol Ester Authors: Zhang, G. / Kazanietz, M.G. / Blumberg, P.M. / Hurley, J.H. #2: ![]() Title: Solution Structure of Cysteine-Rich Domain of Protein Kinase C Alpha Authors: Ichikawa, S. / Hatanaka, H. / Takeuchi, Y. / Ohno, S. / Inagaki, F. #3: ![]() Title: Solution Structure of a Cysteine Rich Domain of Rat Protein Kinase C Authors: Hommel, U. / Zurini, M. / Luyten, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 34.8 KB | Display | ![]() |
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PDB format | ![]() | 23.1 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 294.2 KB | Display | ![]() |
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Full document | ![]() | 293.9 KB | Display | |
Data in XML | ![]() | 3.5 KB | Display | |
Data in CIF | ![]() | 4.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9359.666 Da / Num. of mol.: 1 / Fragment: CYS2 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P05697, UniProt: P63319*PLUS, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 6.5 / Temperature units: K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
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Processing
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NMR software |
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Refinement | Method: DG-SA / Software ordinal: 1 | ||||||||
NMR ensemble | Conformers calculated total number: 1 / Conformers submitted total number: 1 |