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- PDB-4fg8: Crystal structure of human calcium/calmodulin-dependent protein k... -

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Basic information

Entry
Database: PDB / ID: 4fg8
TitleCrystal structure of human calcium/calmodulin-dependent protein kinase I 1-315 in complex with ATP
ComponentsCalcium/calmodulin-dependent protein kinase type 1
KeywordsTRANSFERASE / CaMK / calmodulin / autoinhibition / regulation mechanism / kinase
Function / homology
Function and homology information


positive regulation of syncytium formation by plasma membrane fusion / regulation of protein binding / positive regulation of synapse structural plasticity / regulation of muscle cell differentiation / Ca2+/calmodulin-dependent protein kinase / calcium/calmodulin-dependent protein kinase activity / nucleocytoplasmic transport / positive regulation of dendritic spine development / Activation of RAC1 downstream of NMDARs / positive regulation of muscle cell differentiation ...positive regulation of syncytium formation by plasma membrane fusion / regulation of protein binding / positive regulation of synapse structural plasticity / regulation of muscle cell differentiation / Ca2+/calmodulin-dependent protein kinase / calcium/calmodulin-dependent protein kinase activity / nucleocytoplasmic transport / positive regulation of dendritic spine development / Activation of RAC1 downstream of NMDARs / positive regulation of muscle cell differentiation / regulation of synapse organization / Negative regulation of NMDA receptor-mediated neuronal transmission / positive regulation of protein serine/threonine kinase activity / negative regulation of protein binding / positive regulation of protein export from nucleus / positive regulation of neuron projection development / nervous system development / regulation of protein localization / cell differentiation / calmodulin binding / postsynaptic density / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / signal transduction / positive regulation of transcription by RNA polymerase II / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. ...Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Calcium/calmodulin-dependent protein kinase type 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsZha, M. / Zhong, C. / Ou, Y. / Wang, J. / Han, L. / Ding, J.
CitationJournal: Plos One / Year: 2012
Title: Crystal structures of human CaMKIalpha reveal insights into the regulation mechanism of CaMKI.
Authors: Zha, M. / Zhong, C. / Ou, Y. / Han, L. / Wang, J. / Ding, J.
History
DepositionJun 4, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Calcium/calmodulin-dependent protein kinase type 1
B: Calcium/calmodulin-dependent protein kinase type 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,5464
Polymers71,5312
Non-polymers1,0142
Water2,432135
1
A: Calcium/calmodulin-dependent protein kinase type 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,2732
Polymers35,7661
Non-polymers5071
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Calcium/calmodulin-dependent protein kinase type 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,2732
Polymers35,7661
Non-polymers5071
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)83.415, 83.415, 153.372
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63

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Components

#1: Protein Calcium/calmodulin-dependent protein kinase type 1 / CaM kinase I / CaM-KI / CaM kinase I alpha / CaMKI-alpha


Mass: 35765.699 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CAMK1 / Plasmid: pGEX4T-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q14012, Ca2+/calmodulin-dependent protein kinase
#2: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 135 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.15 Å3/Da / Density % sol: 42.88 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 3% dioxane, 100mM MES, 1.5M (NH4)2SO4, pH 6.0, vapor diffusion, hanging drop, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9791 Å
DetectorType: RAYONIX MX315HE / Detector: CCD / Date: Jan 13, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.805
11h+k,-k,-l20.195
ReflectionResolution: 2.2→76.7 Å / Num. all: 30376 / % possible obs: 99.1 % / Redundancy: 5.5 % / Biso Wilson estimate: 43.4 Å2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 22.4
Reflection shellResolution: 2.2→2.28 Å / % possible all: 99.4

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Processing

Software
NameVersionClassificationNB
REFMAC5.5.0109refinement
PDB_EXTRACT3.11data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4FG7

4fg7


Resolution: 2.2→76.7 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.921 / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.046 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2484 1557 5.1 %RANDOM
Rwork0.1954 ---
obs0.1981 30343 98.97 %-
all-30376 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 184.56 Å2 / Biso mean: 54.5095 Å2 / Biso min: 30.41 Å2
Refinement stepCycle: LAST / Resolution: 2.2→76.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4183 0 62 135 4380
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0224341
X-RAY DIFFRACTIONr_angle_refined_deg1.5881.9785898
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.675525
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.09124.596198
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.01915717
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.7051518
X-RAY DIFFRACTIONCHIRAL-CENTER RESTRAINTS (A''3)0.1310.2657
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0213257
X-RAY DIFFRACTIONMAIN-CHAIN BOND REFINED ATOMS (A''2)1.6321.52642
X-RAY DIFFRACTIONMAIN-CHAIN ANGLE REFINED ATOMS (A''2)2.89424230
X-RAY DIFFRACTIONSIDE-CHAIN BOND REFINED ATOMS (A''2)3.69931699
X-RAY DIFFRACTIONSIDE-CHAIN ANGLE REFINED ATOMS (A''2)5.9944.51668
X-RAY DIFFRACTIONRIGID-BOND RESTRAINTS (A''2)2.03634341
LS refinement shellResolution: 2.199→2.256 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.303 114 -
Rwork0.229 2107 -
all-2221 -
obs--98.01 %

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