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- PDB-9rel: Crystal Structure of the Protein-Kinase A catalytic subunit from ... -

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Basic information

Entry
Database: PDB / ID: 9rel
TitleCrystal Structure of the Protein-Kinase A catalytic subunit from Cricetulus griseus in complex with F283
ComponentscAMP-dependent protein kinase catalytic subunit alpha
KeywordsTRANSFERASE / serine kinase / threonine kinase / small molecules / ligand binding
Function / homology
Function and homology information


cAMP-dependent protein kinase / regulation of protein processing / cAMP-dependent protein kinase activity / protein localization to lipid droplet / regulation of bicellular tight junction assembly / cAMP-dependent protein kinase complex / cellular response to parathyroid hormone stimulus / regulation of osteoblast differentiation / cellular response to cold / sperm capacitation ...cAMP-dependent protein kinase / regulation of protein processing / cAMP-dependent protein kinase activity / protein localization to lipid droplet / regulation of bicellular tight junction assembly / cAMP-dependent protein kinase complex / cellular response to parathyroid hormone stimulus / regulation of osteoblast differentiation / cellular response to cold / sperm capacitation / negative regulation of glycolytic process through fructose-6-phosphate / ciliary base / protein kinase A regulatory subunit binding / intracellular potassium ion homeostasis / mesoderm formation / plasma membrane raft / axoneme / sperm flagellum / postsynaptic modulation of chemical synaptic transmission / regulation of proteasomal protein catabolic process / negative regulation of TORC1 signaling / protein serine/threonine/tyrosine kinase activity / cellular response to glucagon stimulus / positive regulation of gluconeogenesis / acrosomal vesicle / protein export from nucleus / positive regulation of phagocytosis / positive regulation of protein export from nucleus / negative regulation of smoothened signaling pathway / neural tube closure / neuromuscular junction / cellular response to glucose stimulus / positive regulation of cholesterol biosynthetic process / positive regulation of insulin secretion / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / mRNA processing / manganese ion binding / cellular response to heat / postsynapse / regulation of cell cycle / nuclear speck / protein domain specific binding / protein serine kinase activity / protein serine/threonine kinase activity / ubiquitin protein ligase binding / centrosome / protein kinase binding / perinuclear region of cytoplasm / glutamatergic synapse / magnesium ion binding / mitochondrion / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
cAMP-dependent protein kinase catalytic subunit / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / 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. ...cAMP-dependent protein kinase catalytic subunit / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / 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
Similarity search - Domain/homology
Chem-D8V / cAMP-dependent protein kinase catalytic subunit alpha
Similarity search - Component
Biological speciesCricetulus griseus (Chinese hamster)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.42 Å
AuthorsSandner, A. / Mueller, J.M. / Wolter, M. / Glinca, S. / Klebe, G.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: J.Chem.Inf.Model. / Year: 2025
Title: Natural Product-like Fragments Unlock Novel Chemotypes for a Kinase Target Exploring Options beyond the Flatland
Authors: Santura, A. / Muller, J. / Wolter, M. / Tutzschky, I.C. / Ruf, M. / Metz, A. / Sandner, A. / Merkl, S. / Klebe, G. / Glinca, S. / Czodrowski, P.
History
DepositionJun 3, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 31, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: cAMP-dependent protein kinase catalytic subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2739
Polymers41,1141
Non-polymers1,1608
Water5,098283
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1370 Å2
ΔGint11 kcal/mol
Surface area16540 Å2
MethodPISA
Unit cell
Length a, b, c (Å)52.492, 72.284, 98.739
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Space group name HallP2ac2ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x,y+1/2,-z+1/2
#4: -x+1/2,-y,z+1/2

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Components

#1: Protein cAMP-dependent protein kinase catalytic subunit alpha / PKA C-alpha


Mass: 41113.766 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Cricetulus griseus (Chinese hamster) / Gene: PRKACA
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P25321, cAMP-dependent protein kinase
#2: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400


Mass: 238.278 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#3: Chemical ChemComp-D8V / 4-(2-{[methyl(prop-2-yn-1-yl)amino]methyl}-1,3-thiazol-4-yl)piperidin-4-ol


Mass: 265.374 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H19N3OS / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 283 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.28 Å3/Da / Density % sol: 46.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 100 mM Mes/Bis-Tris, 75 mM lithium chloride, 1 mM DTT, 0.1 mM sodium EDTA, 0.25 mM Mega 8, 23% v/v methanol/water in reservoir

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184 Å
DetectorType: DECTRIS PILATUS3 2M / Detector: PIXEL / Date: Oct 25, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 1.42→46.35 Å / Num. obs: 71553 / % possible obs: 99.9 % / Redundancy: 5.9 % / Biso Wilson estimate: 17.7 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.063 / Net I/σ(I): 11.7
Reflection shellResolution: 1.42→1.44 Å / Redundancy: 6.1 % / Rmerge(I) obs: 1.056 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 3482 / CC1/2: 0.719 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.21.2_5419refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.42→24.68 Å / SU ML: 0.1813 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 16.7443
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1773 3598 5.04 %
Rwork0.1569 67851 -
obs0.1579 71449 99.81 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 22 Å2
Refinement stepCycle: LAST / Resolution: 1.42→24.68 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2774 0 72 283 3129
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02073123
X-RAY DIFFRACTIONf_angle_d1.42714246
X-RAY DIFFRACTIONf_chiral_restr0.1189435
X-RAY DIFFRACTIONf_plane_restr0.0119546
X-RAY DIFFRACTIONf_dihedral_angle_d20.92721162
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.42-1.440.47071360.42962576X-RAY DIFFRACTION99.82
1.44-1.460.37541460.35022556X-RAY DIFFRACTION99.89
1.46-1.480.27261650.2662559X-RAY DIFFRACTION99.96
1.48-1.50.23191340.22032584X-RAY DIFFRACTION99.89
1.5-1.520.22271170.18262585X-RAY DIFFRACTION99.96
1.52-1.550.21011310.16792618X-RAY DIFFRACTION99.78
1.55-1.580.18871160.14452571X-RAY DIFFRACTION100
1.58-1.610.19541530.13762578X-RAY DIFFRACTION100
1.61-1.640.20251300.14372597X-RAY DIFFRACTION99.96
1.64-1.670.1851310.14582587X-RAY DIFFRACTION99.85
1.67-1.710.20371300.152593X-RAY DIFFRACTION99.63
1.71-1.750.20141280.15462600X-RAY DIFFRACTION99.31
1.75-1.790.18571340.13582556X-RAY DIFFRACTION98.97
1.79-1.840.14091460.1332571X-RAY DIFFRACTION99.96
1.84-1.890.16121310.1282618X-RAY DIFFRACTION100
1.89-1.950.16031460.13922605X-RAY DIFFRACTION99.82
1.95-2.020.16951370.13612629X-RAY DIFFRACTION99.96
2.02-2.10.17721410.1392598X-RAY DIFFRACTION99.96
2.1-2.20.17511340.14352613X-RAY DIFFRACTION99.96
2.2-2.310.16741290.14672613X-RAY DIFFRACTION99.64
2.31-2.460.18141400.14652617X-RAY DIFFRACTION99.82
2.46-2.650.15691440.15772641X-RAY DIFFRACTION99.79
2.65-2.920.19451470.16922642X-RAY DIFFRACTION99.89
2.92-3.340.17621460.17072653X-RAY DIFFRACTION99.93
3.34-4.20.15711350.14752699X-RAY DIFFRACTION100
4.2-24.680.16181710.16082792X-RAY DIFFRACTION99.43

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