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- PDB-1nuk: CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEP... -

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Basic information

Entry
Database: PDB / ID: 1nuk
TitleCRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE
ComponentsPROTEIN (TYROSINE-PROTEIN KINASE RECEPTOR EPH)
KeywordsTRANSFERASE / EPH RECEPTOR TYROSINE KINASE
Function / homology
Function and homology information


regulation of T-helper 17 type immune response / Ephrin signaling / EPH-Ephrin signaling / hindbrain tangential cell migration / negative regulation of glutamate receptor signaling pathway / vesicle-mediated intercellular transport / EPH-ephrin mediated repulsion of cells / EPHB-mediated forward signaling / optic nerve morphogenesis / urogenital system development ...regulation of T-helper 17 type immune response / Ephrin signaling / EPH-Ephrin signaling / hindbrain tangential cell migration / negative regulation of glutamate receptor signaling pathway / vesicle-mediated intercellular transport / EPH-ephrin mediated repulsion of cells / EPHB-mediated forward signaling / optic nerve morphogenesis / urogenital system development / tight junction assembly / regulation of body fluid levels / neuron projection retraction / central nervous system projection neuron axonogenesis / postsynaptic membrane assembly / axon guidance receptor activity / transmembrane-ephrin receptor activity / negative regulation of axonogenesis / positive regulation of synaptic plasticity / positive regulation of long-term neuronal synaptic plasticity / corpus callosum development / dendritic spine development / camera-type eye morphogenesis / regulation of filopodium assembly / ephrin receptor activity / positive regulation of dendritic spine morphogenesis / positive regulation of glutamate receptor signaling pathway / regulation of behavioral fear response / regulation of autophagosome assembly / commissural neuron axon guidance / dendritic spine morphogenesis / negative regulation of Ras protein signal transduction / negative regulation of cell adhesion / positive regulation of protein localization to cell surface / axonal fasciculation / phosphorylation / retinal ganglion cell axon guidance / positive regulation of synapse assembly / regulation of receptor signaling pathway via JAK-STAT / positive regulation of immunoglobulin production / inner ear morphogenesis / regulation of axonogenesis / regulation of synapse assembly / regulation of blood coagulation / B cell activation / roof of mouth development / regulation of neuronal synaptic plasticity / ephrin receptor signaling pathway / positive regulation of B cell proliferation / neuron projection maintenance / negative regulation of cytokine production involved in inflammatory response / axonogenesis / axon guidance / cell surface receptor protein tyrosine kinase signaling pathway / peptidyl-tyrosine phosphorylation / hippocampal mossy fiber to CA3 synapse / animal organ morphogenesis / positive regulation of long-term synaptic potentiation / learning / receptor protein-tyrosine kinase / negative regulation of ERK1 and ERK2 cascade / cellular response to amyloid-beta / cell morphogenesis / positive regulation of tumor necrosis factor production / signaling receptor activity / amyloid-beta binding / cellular response to lipopolysaccharide / presynaptic membrane / protein tyrosine kinase activity / angiogenesis / dendritic spine / postsynaptic membrane / learning or memory / positive regulation of cell migration / signaling receptor binding / axon / neuronal cell body / synapse / dendrite / protein-containing complex binding / glutamatergic synapse / cell surface / nucleoplasm / ATP binding / identical protein binding / plasma membrane
Similarity search - Function
Ephrin type-B receptor 2, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / : / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain ...Ephrin type-B receptor 2, ligand binding domain / Tyrosine-protein kinase ephrin type A/B receptor-like / Tyrosine-protein kinase ephrin type A/B receptor-like / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / : / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. / Ephrin receptor ligand binding domain / Putative ephrin-receptor like / SAM domain (Sterile alpha motif) / Galactose-binding domain-like / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Fibronectin type III domain / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Jelly Rolls / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Sandwich / Mainly Beta
Similarity search - Domain/homology
Ephrin type-B receptor 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / MIR / Resolution: 2.9 Å
AuthorsHimanen, J.-P. / Henkemeyer, M. / Nikolov, D.B.
CitationJournal: Nature / Year: 1998
Title: Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2.
Authors: Himanen, J.P. / Henkemeyer, M. / Nikolov, D.B.
History
DepositionOct 13, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Oct 13, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 27, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (TYROSINE-PROTEIN KINASE RECEPTOR EPH)


Theoretical massNumber of molelcules
Total (without water)21,1401
Polymers21,1401
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)55.150, 55.150, 158.900
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein PROTEIN (TYROSINE-PROTEIN KINASE RECEPTOR EPH) / NUK


Mass: 21139.881 Da / Num. of mol.: 1 / Fragment: LIGAND-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / Strain (production host): AD494 / References: UniProt: P54763, EC: 2.7.1.112
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.86 Å3/Da / Density % sol: 56.94 %
Crystal growpH: 5 / Details: pH 5.0
Crystal grow
*PLUS
pH: 7.2 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlprotein1drop
210 mM1dropKCl
32 mM1dropMgCl2
410 mMHEPES1drop
5200 mMammonium sulfate1reservoir
615 %PEG40001reservoir
750 mMsodium acetate1reservoir

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Data collection

DiffractionMean temperature: 290 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.9→8 Å / Num. obs: 4214 / % possible obs: 95 % / Observed criterion σ(I): 2 / Redundancy: 5 % / Rmerge(I) obs: 0.11 / Rsym value: 0.11
Reflection
*PLUS
Redundancy: 5 %

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Processing

SoftwareName: X-PLOR / Version: 3.1 / Classification: refinement
RefinementMethod to determine structure: MIR / Resolution: 2.9→8 Å / σ(F): 2
RfactorNum. reflection% reflection
Rfree0.314 340 7.5 %
Rwork0.206 --
obs0.206 4554 80 %
Displacement parametersBiso mean: 24.9 Å2
Refinement stepCycle: LAST / Resolution: 2.9→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1362 0 0 0 1362
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.012
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.97
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Version: 3.1 / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.9 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 7.5 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 24.9 Å2

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