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- PDB-2x11: Crystal structure of the complete EphA2 ectodomain in complex wit... -

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Basic information

Entry
Database: PDB / ID: 2x11
TitleCrystal structure of the complete EphA2 ectodomain in complex with ephrin A5 receptor binding domain
Components
  • EPHRIN TYPE-A RECEPTOR 2
  • EPHRIN-A5
KeywordsRECEPTOR/SIGNALING PROTEIN / RECEPTOR-SIGNALING PROTEIN COMPLEX / DEVELOPMENTAL PROTEIN / SIGNALING PLATFORM / KINASE / TRANSFERASE / NEUROGENESIS / RECEPTOR / CATARACT / APOPTOSIS / ERYTHROPOIETIN-PRODUCING HEPATOCELLULAR CARCINOMA / ANGIOGENESIS / SIGNALING PROTEIN
Function / homology
Function and homology information


neurotrophin TRKC receptor binding / neurotrophin TRKB receptor binding / negative regulation of substrate adhesion-dependent cell spreading / notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / synaptic membrane adhesion / axial mesoderm formation ...neurotrophin TRKC receptor binding / neurotrophin TRKB receptor binding / negative regulation of substrate adhesion-dependent cell spreading / notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / synaptic membrane adhesion / axial mesoderm formation / pericyte cell differentiation / cAMP metabolic process / collateral sprouting / cellular response to follicle-stimulating hormone stimulus / regulation of blood vessel endothelial cell migration / leading edge membrane / positive regulation of collateral sprouting / regulation of insulin secretion involved in cellular response to glucose stimulus / negative regulation of chemokine production / neurotrophin TRKA receptor binding / post-anal tail morphogenesis / response to growth factor / transmembrane receptor protein tyrosine kinase activator activity / chemorepellent activity / bone remodeling / positive regulation of bicellular tight junction assembly / activation of GTPase activity / regulation of lamellipodium assembly / regulation of cell morphogenesis / branching involved in mammary gland duct morphogenesis / positive regulation of synapse assembly / EPH-Ephrin signaling / tight junction / RND1 GTPase cycle / neural tube development / RND2 GTPase cycle / RND3 GTPase cycle / regulation of GTPase activity / mammary gland epithelial cell proliferation / regulation of focal adhesion assembly / positive regulation of peptidyl-tyrosine phosphorylation / retinal ganglion cell axon guidance / RHOV GTPase cycle / EPHA-mediated growth cone collapse / growth factor binding / regulation of cell adhesion mediated by integrin / regulation of cell-cell adhesion / lamellipodium membrane / RHOU GTPase cycle / basement membrane / RHOG GTPase cycle / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / RAC2 GTPase cycle / RAC3 GTPase cycle / regulation of angiogenesis / regulation of ERK1 and ERK2 cascade / vasculogenesis / keratinocyte differentiation / ephrin receptor binding / transmembrane receptor protein tyrosine kinase activity / RAC1 GTPase cycle / cellular response to forskolin / regulation of microtubule cytoskeleton organization / osteoclast differentiation / axon guidance / cell surface receptor protein tyrosine kinase signaling pathway / negative regulation of angiogenesis / molecular function activator activity / protein localization to plasma membrane / skeletal system development / GABA-ergic synapse / cell chemotaxis / adherens junction / positive regulation of protein localization to plasma membrane / regulation of actin cytoskeleton organization / cell motility / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / caveola / ruffle membrane / intrinsic apoptotic signaling pathway in response to DNA damage / neuron differentiation / osteoblast differentiation / cell migration
Similarity search - Function
Ephrin-A ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) domain profile. / Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain ...Ephrin-A ectodomain / Ephrin receptor-binding domain / Ephrin, conserved site / Ephrin / Ephrin / Ephrin receptor-binding (ephrin RBD) domain signature. / Ephrin receptor-binding (ephrin RBD) domain profile. / Ephrin type-A receptor 2, ligand binding domain / 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) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Cupredoxin / 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 / 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
Similarity search - Domain/homology
Ephrin type-A receptor 2 / Ephrin-A5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.83 Å
AuthorsSeiradake, E. / Harlos, K. / Sutton, G. / Aricescu, A.R. / Jones, E.Y.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: An Extracellular Steric Seeding Mechanism for Eph-Ephrin Signalling Platform Assembly
Authors: Seiradake, E. / Harlos, K. / Sutton, G. / Aricescu, A.R. / Jones, E.Y.
History
DepositionDec 21, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 16, 2010Provider: repository / Type: Initial release
Revision 1.1Aug 31, 2011Group: Database references / Derived calculations ...Database references / Derived calculations / Refinement description / Version format compliance
Revision 1.2Feb 28, 2018Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.gene_src_common_name / _entity_src_gen.host_org_common_name ..._entity_src_gen.gene_src_common_name / _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Revision 1.4Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EPHRIN TYPE-A RECEPTOR 2
B: EPHRIN-A5


Theoretical massNumber of molelcules
Total (without water)80,2622
Polymers80,2622
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1980 Å2
ΔGint-11.6 kcal/mol
Surface area33010 Å2
MethodPISA
Unit cell
Length a, b, c (Å)173.630, 59.630, 112.160
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number17
Space group name H-MP2221

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Components

#1: Protein EPHRIN TYPE-A RECEPTOR 2 / TYROSINE-PROTEIN KINASE RECEPTOR ECK / EPITHELIAL CELL KINASE / EPHA2


Mass: 59859.215 Da / Num. of mol.: 1 / Fragment: ECTODOMAIN, RESIDUES 27-534
Source method: isolated from a genetically manipulated source
Details: NAG ON ASN407, DI-METHYLATION OF LYSINES / Source: (gene. exp.) Homo sapiens (human) / Plasmid: PHLSEC / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / Variant (production host): GNTI-DEFICIENT
References: UniProt: P29317, receptor protein-tyrosine kinase
#2: Protein EPHRIN-A5 / EPH-RELATED RECEPTOR TYROSINE KINASE LIGAND 7 / LERK-7 / AL-1 / HUMAN EPHRIN A5


Mass: 20402.324 Da / Num. of mol.: 1 / Fragment: RECEPTOR BINDING DOMAIN, RESIDUES 26-166
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PHLSEC / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / Variant (production host): GNTI-DEFICIENT / References: UniProt: P52803
Has protein modificationY
Sequence detailsCONTAINS FOREIGN SIGNAL PEPTIDE AND POLY-HIS TAG

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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: 3.61 Å3/Da / Density % sol: 66 % / Description: NONE
Crystal growDetails: TWO PARTS OF PROTEIN SOLUTION WERE MIXED WITH ONE PART WATER, ONE PART RESERVOIR SOLUTION (8 % POLYETHYLENE GLYCOL 6000, 0.8 M LICL, 0.08 M CITRATE PH 5) AND ONE PART 1 % POLYVINYLPYRROLIDONE K15.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 13, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 4.8→173 Å / Num. obs: 6016 / % possible obs: 98.2 % / Observed criterion σ(I): 1 / Redundancy: 6.2 % / Biso Wilson estimate: 166.11 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 12.95
Reflection shellResolution: 4.8→4.9 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.74 / Mean I/σ(I) obs: 2.8 / % possible all: 75.7

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3CZU, 3FL7, 1SHW

3czu

3fl7

1shw


Resolution: 4.83→40.482 Å / σ(F): 0.03 / Phase error: 34 / Stereochemistry target values: ML
Details: DUE TO LOW RESOLUTION, THE REFINEMENT PROTOCOL WAS LIMITED TO THE FOLLOWING THREE STEPS AFTER MOLECULAR REPLACEMENT. 1. RIGID BODY REFINEMENT OF INDIVIDUAL DOMAINS 2. TLS REFINEMENT OF ...Details: DUE TO LOW RESOLUTION, THE REFINEMENT PROTOCOL WAS LIMITED TO THE FOLLOWING THREE STEPS AFTER MOLECULAR REPLACEMENT. 1. RIGID BODY REFINEMENT OF INDIVIDUAL DOMAINS 2. TLS REFINEMENT OF SELECTED PORTIONS 3. STRUCTURE REGULARIZATION TO AVOID MINOR CLASHES. WE PERFORMED NO INDIVIDUAL ATOM REFINEMENT.
RfactorNum. reflection% reflection
Rfree0.3143 260 4.6 %
Rwork0.3123 --
obs0.313 5643 93.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 99 Å2 / ksol: 0.298 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--46.5561 Å2-0 Å20 Å2
2---4.8023 Å20 Å2
3---48.1254 Å2
Refinement stepCycle: LAST / Resolution: 4.83→40.482 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4870 0 0 0 4870
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0035039
X-RAY DIFFRACTIONf_angle_d0.6756844
X-RAY DIFFRACTIONf_dihedral_angle_d17.7071778
X-RAY DIFFRACTIONf_chiral_restr0.044729
X-RAY DIFFRACTIONf_plane_restr0.004901
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.8261-6.07710.33411170.34012537X-RAY DIFFRACTION90
6.0771-40.4830.30741430.30122846X-RAY DIFFRACTION97

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