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- PDB-5cwz: Crystal structure of the kinase domain of human TRAF2 and NCK-int... -

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Basic information

Entry
Database: PDB / ID: 5cwz
TitleCrystal structure of the kinase domain of human TRAF2 and NCK-interacting protein kinase
ComponentsTRAF2 and NCK-interacting protein kinase
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / kinase / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


microvillus assembly / regulation of dendrite morphogenesis / regulation of MAPK cascade / postsynaptic density, intracellular component / neuron projection morphogenesis / cytoskeleton organization / protein localization to plasma membrane / positive regulation of JNK cascade / recycling endosome / Wnt signaling pathway ...microvillus assembly / regulation of dendrite morphogenesis / regulation of MAPK cascade / postsynaptic density, intracellular component / neuron projection morphogenesis / cytoskeleton organization / protein localization to plasma membrane / positive regulation of JNK cascade / recycling endosome / Wnt signaling pathway / positive regulation of protein phosphorylation / presynapse / MAPK cascade / protein autophosphorylation / actin cytoskeleton organization / Oxidative Stress Induced Senescence / cytoskeleton / protein phosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / apical plasma membrane / protein serine kinase activity / protein serine/threonine kinase activity / glutamatergic synapse / extracellular exosome / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol
Similarity search - Function
: / Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2 / CNH domain / Citron homology (CNH) domain / Citron homology (CNH) domain profile. / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site ...: / Domain found in NIK1-like kinases, mouse citron and yeast ROM1, ROM2 / CNH domain / Citron homology (CNH) domain / Citron homology (CNH) domain profile. / 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
TRAF2 and NCK-interacting protein kinase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsOhbayashi, N. / Kukimoto-Niino, M. / Yamada, T. / Shirouzu, M.
CitationJournal: Nat Commun / Year: 2016
Title: TNIK inhibition abrogates colorectal cancer stemness
Authors: Masuda, M. / Uno, Y. / Ohbayashi, N. / Ohata, H. / Mimata, A. / Kukimoto-Niino, M. / Moriyama, H. / Kashimoto, S. / Inoue, T. / Goto, N. / Okamoto, K. / Shirouzu, M. / Sawa, M. / Yamada, T.
History
DepositionJul 28, 2015Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jul 27, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 7, 2016Group: Database references
Revision 1.2Feb 19, 2020Group: Data collection / Derived calculations / Category: diffrn_source / pdbx_struct_oper_list
Item: _diffrn_source.pdbx_synchrotron_site / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Nov 8, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRAF2 and NCK-interacting protein kinase
B: TRAF2 and NCK-interacting protein kinase
C: TRAF2 and NCK-interacting protein kinase


Theoretical massNumber of molelcules
Total (without water)105,2293
Polymers105,2293
Non-polymers00
Water362
1
A: TRAF2 and NCK-interacting protein kinase


Theoretical massNumber of molelcules
Total (without water)35,0761
Polymers35,0761
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: TRAF2 and NCK-interacting protein kinase


Theoretical massNumber of molelcules
Total (without water)35,0761
Polymers35,0761
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: TRAF2 and NCK-interacting protein kinase


Theoretical massNumber of molelcules
Total (without water)35,0761
Polymers35,0761
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)50.215, 123.896, 158.450
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121

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Components

#1: Protein TRAF2 and NCK-interacting protein kinase


Mass: 35076.328 Da / Num. of mol.: 3 / Fragment: UNP residues 11-314
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNIK, KIAA0551 / Production host: Baculovirus expression vector pFastBac1-HM
References: UniProt: Q9UKE5, non-specific serine/threonine protein kinase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.44 Å3/Da / Density % sol: 49.54 %
Description: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.2
Details: 0.2M Ammonium sulfate, 0.1M Bis-tris (6.2), 35% PEG3350, 9% Ethylene glycol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B2 / Wavelength: 1 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Apr 21, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.9→48.59 Å / Num. obs: 22760 / % possible obs: 100 % / Redundancy: 7.3 % / Net I/σ(I): 18.2
Reflection shellResolution: 2.9→3.08 Å / Redundancy: 7.5 % / Rmerge(I) obs: 0.692 / Mean I/σ(I) obs: 3.4 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2X7F

2x7f


Resolution: 2.9→48.586 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 31.49 / Stereochemistry target values: ML
Details: SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS COLUMNS.
RfactorNum. reflection% reflection
Rfree0.2814 1161 5.12 %
Rwork0.2086 --
obs0.2123 22686 99.8 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.9→48.586 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6724 0 0 2 6726
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0046872
X-RAY DIFFRACTIONf_angle_d0.7919274
X-RAY DIFFRACTIONf_dihedral_angle_d12.8532607
X-RAY DIFFRACTIONf_chiral_restr0.031008
X-RAY DIFFRACTIONf_plane_restr0.0041195
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9-3.0320.36511450.27232639X-RAY DIFFRACTION100
3.032-3.19180.31471230.25262676X-RAY DIFFRACTION100
3.1918-3.39180.32271480.23892624X-RAY DIFFRACTION100
3.3918-3.65360.32011340.22162662X-RAY DIFFRACTION100
3.6536-4.02110.29621690.20792634X-RAY DIFFRACTION100
4.0211-4.60250.26281380.17642716X-RAY DIFFRACTION100
4.6025-5.79720.25331460.2012708X-RAY DIFFRACTION100
5.7972-48.59290.25011580.19792866X-RAY DIFFRACTION100

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