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- PDB-2ux0: Structure of the oligomerisation domain of calcium-calmodulin dep... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ux0 | ||||||
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Title | Structure of the oligomerisation domain of calcium-calmodulin dependent protein kinase II gamma | ||||||
![]() | CALCIUM-CALMODULIN DEPENDENT PROTEIN KINASE (CAM KINASE) II GAMMA | ||||||
![]() | TRANSFERASE / CALMODULIN / PROTEIN KINASE / OLIGOMERISATION DOMAIN / SERINE- THREONINE KINASE / ATP-BINDING / KINASE / NUCLEOTIDE-BINDING / SERINE/THREONINE-PROTEIN KINASE / TRANSFERASE. | ||||||
Function / homology | ![]() regulation of skeletal muscle adaptation / calcium-dependent protein serine/threonine phosphatase activity / calcium- and calmodulin-dependent protein kinase complex / Ca2+/calmodulin-dependent protein kinase / Trafficking of AMPA receptors / Assembly and cell surface presentation of NMDA receptors / insulin secretion / calcium/calmodulin-dependent protein kinase activity / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / regulation of neuron projection development ...regulation of skeletal muscle adaptation / calcium-dependent protein serine/threonine phosphatase activity / calcium- and calmodulin-dependent protein kinase complex / Ca2+/calmodulin-dependent protein kinase / Trafficking of AMPA receptors / Assembly and cell surface presentation of NMDA receptors / insulin secretion / calcium/calmodulin-dependent protein kinase activity / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / regulation of neuron projection development / CaMK IV-mediated phosphorylation of CREB / Negative regulation of NMDA receptor-mediated neuronal transmission / Unblocking of NMDA receptors, glutamate binding and activation / Phase 0 - rapid depolarisation / regulation of calcium ion transport / Ion transport by P-type ATPases / Long-term potentiation / Regulation of MECP2 expression and activity / HSF1-dependent transactivation / Ion homeostasis / sarcoplasmic reticulum membrane / Ras activation upon Ca2+ influx through NMDA receptor / RAF activation / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / endocytic vesicle membrane / Interferon gamma signaling / Signaling by BRAF and RAF1 fusions / nervous system development / RAF/MAP kinase cascade / cell differentiation / calmodulin binding / neuron projection / phosphorylation / protein serine kinase activity / protein homodimerization activity / nucleoplasm / ATP binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bunkoczi, G. / Debreczeni, J.E. / Salah, E. / Gileadi, O. / Rellos, P. / Arrowsmith, C.H. / Edwards, A. / Sundstrom, M. / Weigelt, J. / von Delft, F. ...Bunkoczi, G. / Debreczeni, J.E. / Salah, E. / Gileadi, O. / Rellos, P. / Arrowsmith, C.H. / Edwards, A. / Sundstrom, M. / Weigelt, J. / von Delft, F. / Turnbull, A. / Pike, A.C.W. / Knapp, S. | ||||||
![]() | ![]() Title: Structure of the Camkiidelta/Calmodulin Complex Reveals the Molecular Mechanism of Camkii Kinase Activation. Authors: Rellos, P. / Pike, A.C.W. / Niesen, F.H. / Salah, E. / Lee, W.H. / von Delft, F. / Knapp, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 170.4 KB | Display | ![]() |
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PDB format | ![]() | 136.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 486 KB | Display | ![]() |
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Full document | ![]() | 493.5 KB | Display | |
Data in XML | ![]() | 30.9 KB | Display | |
Data in CIF | ![]() | 41.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2v7oC ![]() 2vn9C ![]() 2vz6C ![]() 2w2cC ![]() 2welC ![]() 1hkxS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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Components
#1: Protein | Mass: 16375.393 Da / Num. of mol.: 6 / Fragment: OLIGOMERISATION DOMAIN, RESIDUES 387-527 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q8N4I3, UniProt: Q13555*PLUS, EC: 2.7.1.123 #2: Chemical | ChemComp-GLY / #3: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, LEU 526 TO ARG ENGINEERED RESIDUE IN CHAIN B, LEU 526 TO ARG ...ENGINEERED | Sequence details | THE L526R MUTATION IS FROM THE ENTRY CLONE THAT HAS BEEN SEQUENCED AFTER IDENTIFICA | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53 % |
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Crystal grow | pH: 7 / Details: 0.1 M SPG PH 7.0, 60% MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 21, 2006 |
Radiation | Monochromator: SI111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9999 Å / Relative weight: 1 |
Reflection | Resolution: 2.46→39.7 Å / Num. obs: 29117 / % possible obs: 78.2 % / Observed criterion σ(I): 0 / Redundancy: 2.63 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.46→2.56 Å / Redundancy: 0.13 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 1.45 / % possible all: 10.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HKX Resolution: 2.46→39.68 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.937 / SU B: 21.332 / SU ML: 0.211 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.982 / ESU R Free: 0.295 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.13 Å2
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Refinement step | Cycle: LAST / Resolution: 2.46→39.68 Å
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Refine LS restraints |
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