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- PDB-5c03: Crystal Structure of kinase -

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Basic information

Entry
Database: PDB / ID: 5c03
TitleCrystal Structure of kinase
ComponentsNon-receptor tyrosine-protein kinase TYK2
KeywordsTRANSFERASE / pseudokinase domain
Function / homology
Function and homology information


Interleukin-23 signaling / positive regulation of NK T cell proliferation / type 1 angiotensin receptor binding / Interleukin-27 signaling / IL-6-type cytokine receptor ligand interactions / Interleukin-35 Signalling / positive regulation of natural killer cell proliferation / growth hormone receptor binding / Interleukin-12 signaling / type I interferon signaling pathway ...Interleukin-23 signaling / positive regulation of NK T cell proliferation / type 1 angiotensin receptor binding / Interleukin-27 signaling / IL-6-type cytokine receptor ligand interactions / Interleukin-35 Signalling / positive regulation of natural killer cell proliferation / growth hormone receptor binding / Interleukin-12 signaling / type I interferon signaling pathway / Interleukin-6 signaling / Interleukin-20 family signaling / Other interleukin signaling / MAPK3 (ERK1) activation / MAPK1 (ERK2) activation / Interleukin-10 signaling / Regulation of IFNA signaling / Signaling by CSF3 (G-CSF) / positive regulation of T cell proliferation / positive regulation of receptor signaling pathway via JAK-STAT / Interferon alpha/beta signaling / Inactivation of CSF3 (G-CSF) signaling / non-specific protein-tyrosine kinase / cytokine-mediated signaling pathway / non-membrane spanning protein tyrosine kinase activity / positive regulation of interferon-gamma production / Potential therapeutics for SARS / protein tyrosine kinase activity / Interleukin-4 and Interleukin-13 signaling / cytoskeleton / intracellular signal transduction / protein phosphorylation / protein serine/threonine/tyrosine kinase activity / extracellular exosome / membrane / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Tyrosine-protein kinase, non-receptor, TYK2, N-terminal / FERM F1 ubiquitin-like domain / FERM F2 acyl-CoA binding protein-like domain / Jak1 pleckstrin homology-like domain / JAK1-3/TYK2, pleckstrin homology-like domain / FERM F1 lobe ubiquitin-like domain / JAK, FERM F2 lobe domain / Tyrosine-protein kinase, non-receptor Jak/Tyk2 / FERM superfamily, second domain / FERM domain profile. ...Tyrosine-protein kinase, non-receptor, TYK2, N-terminal / FERM F1 ubiquitin-like domain / FERM F2 acyl-CoA binding protein-like domain / Jak1 pleckstrin homology-like domain / JAK1-3/TYK2, pleckstrin homology-like domain / FERM F1 lobe ubiquitin-like domain / JAK, FERM F2 lobe domain / Tyrosine-protein kinase, non-receptor Jak/Tyk2 / FERM superfamily, second domain / FERM domain profile. / FERM domain / Band 4.1 domain / Band 4.1 homologues / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / 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
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / Non-receptor tyrosine-protein kinase TYK2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsMin, X. / Wang, Z. / Walker, N.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: Structural and Functional Characterization of the JH2 Pseudokinase Domain of JAK Family Tyrosine Kinase 2 (TYK2).
Authors: Min, X. / Ungureanu, D. / Maxwell, S. / Hammaren, H. / Thibault, S. / Hillert, E.K. / Ayres, M. / Greenfield, B. / Eksterowicz, J. / Gabel, C. / Walker, N. / Silvennoinen, O. / Wang, Z.
History
DepositionJun 12, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 16, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 23, 2015Group: Database references
Revision 1.2Nov 18, 2015Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Non-receptor tyrosine-protein kinase TYK2
B: Non-receptor tyrosine-protein kinase TYK2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,87917
Polymers76,9512
Non-polymers1,92815
Water5,368298
1
A: Non-receptor tyrosine-protein kinase TYK2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,4869
Polymers38,4761
Non-polymers1,0108
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Non-receptor tyrosine-protein kinase TYK2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3938
Polymers38,4761
Non-polymers9187
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)56.120, 47.690, 112.750
Angle α, β, γ (deg.)90.000, 93.720, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Non-receptor tyrosine-protein kinase TYK2


Mass: 38475.527 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TYK2 / Plasmid: pFASTBac / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P29597, non-specific protein-tyrosine kinase

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Non-polymers , 5 types, 313 molecules

#2: Chemical ChemComp-AGS / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-GAMMA-S / ADENOSINE 5'-(3-THIOTRIPHOSPHATE) / ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE) / ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE


Mass: 523.247 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O12P3S / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 298 / 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: 2.12 Å3/Da / Density % sol: 42 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 / Details: 18-22% PEG 4000, 0.1 M Tris, pH 8.5, 200 mM CaCl2 / Temp details: K

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Data collection

DiffractionMean temperature: 100 K / Ambient temp details: single-wavelength
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 26, 2010
RadiationMonochromator: Double-crystal Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→112.512 Å / Num. all: 47018 / Num. obs: 47018 / % possible obs: 99.4 % / Redundancy: 3.4 % / Rpim(I) all: 0.051 / Rrim(I) all: 0.097 / Rsym value: 0.082 / Net I/av σ(I): 6.866 / Net I/σ(I): 9.9 / Num. measured all: 161958
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRpim(I) allRsym valueNet I/σ(I) obs% possible all
1.9-23.50.5031.32375268300.3130.5032.999.5
2-2.123.50.3032.22217364100.1880.3034.399.3
2.12-2.273.50.2063.22118761130.1280.2066.199.5
2.27-2.453.40.1345.21949356640.0840.1347.799.5
2.45-2.693.50.1016.71798052020.0630.1019.899.4
2.69-33.50.0778.71641747240.0480.07712.399.5
3-3.473.50.06110.21463141790.0380.06116.599.3
3.47-4.253.40.04911.81197535660.0310.0492099.2
4.25-6.013.20.04412.5889327410.0280.04420.198.6
6.01-47.693.40.03914.1545715890.0250.03920.699.7

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Processing

Software
NameVersionClassification
REFMAC5.7.0029refinement
PDB_EXTRACT3.14data extraction
SCALAdata scaling
PHASERphasing
MOSFLMdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→30 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.934 / WRfactor Rfree: 0.2172 / WRfactor Rwork: 0.1813 / FOM work R set: 0.871 / SU B: 3.083 / SU ML: 0.09 / SU R Cruickshank DPI: 0.1466 / SU Rfree: 0.1356 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.147 / ESU R Free: 0.136 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2185 2380 5.1 %RANDOM
Rwork0.1815 44577 --
obs0.1833 46957 99.16 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 77.12 Å2 / Biso mean: 25.981 Å2 / Biso min: 5.43 Å2
Baniso -1Baniso -2Baniso -3
1-0.67 Å20 Å2-0.3 Å2
2---0.23 Å20 Å2
3----0.42 Å2
Refinement stepCycle: final / Resolution: 1.9→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4129 0 118 298 4545
Biso mean--27.77 32.63 -
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0194358
X-RAY DIFFRACTIONr_bond_other_d0.0010.024174
X-RAY DIFFRACTIONr_angle_refined_deg1.2761.9895909
X-RAY DIFFRACTIONr_angle_other_deg0.75139585
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.5435521
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.41822.615195
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.72915727
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.0161542
X-RAY DIFFRACTIONr_chiral_restr0.0730.2660
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0214783
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021013
LS refinement shellResolution: 1.9→1.949 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.236 188 -
Rwork0.243 3231 -
all-3419 -
obs--98.96 %

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