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- PDB-4bka: crystal structure of the human EphA4 ectodomain in complex with h... -
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Basic information
Entry | Database: PDB / ID: 4bka | ||||||
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Title | crystal structure of the human EphA4 ectodomain in complex with human ephrin A5 | ||||||
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![]() | CELL ADHESION / CELL REPULSION / RECEPTOR CLUSTERING / RECEPTOR CIS INTERACTION / EPH-EPHRIN / EPH ECTODOMAIN / ERYTHROPOETIN-PRODUCING HEPATOCELLULAR RECEPTOR / LBD / SUSHI / EGF / FN | ||||||
Function / homology | ![]() neurotrophin TRKC receptor binding / neurotrophin TRKB receptor binding / DH domain binding / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / neuron projection guidance / nephric duct morphogenesis ...neurotrophin TRKC receptor binding / neurotrophin TRKB receptor binding / DH domain binding / neuron projection fasciculation / positive regulation of Rho guanyl-nucleotide exchange factor activity / corticospinal tract morphogenesis / regulation of astrocyte differentiation / negative regulation of proteolysis involved in protein catabolic process / neuron projection guidance / nephric duct morphogenesis / regulation of synapse pruning / fasciculation of sensory neuron axon / fasciculation of motor neuron axon / synapse pruning / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / negative regulation of cellular response to hypoxia / negative regulation of substrate adhesion-dependent cell spreading / negative regulation of axon regeneration / glial cell migration / regulation of cell-cell adhesion / synaptic membrane adhesion / PH domain binding / GPI-linked ephrin receptor activity / regulation of modification of synaptic structure / cellular response to follicle-stimulating hormone stimulus / collateral sprouting / positive regulation of collateral sprouting / regulation of insulin secretion involved in cellular response to glucose stimulus / regulation of dendritic spine morphogenesis / chemorepellent activity / neurotrophin TRKA receptor binding / transmembrane-ephrin receptor activity / negative regulation of cell adhesion / negative regulation of epithelial to mesenchymal transition / regulation of cell morphogenesis / adult walking behavior / motor neuron axon guidance / positive regulation of synapse assembly / adherens junction organization / positive regulation of dendrite morphogenesis / EPH-Ephrin signaling / Somitogenesis / regulation of focal adhesion assembly / retinal ganglion cell axon guidance / positive regulation of amyloid-beta formation / regulation of axonogenesis / cochlea development / regulation of GTPase activity / EPHA-mediated growth cone collapse / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of protein tyrosine kinase activity / positive regulation of cell adhesion / negative regulation of long-term synaptic potentiation / basement membrane / EPH-ephrin mediated repulsion of cells / GABA-ergic synapse / ephrin receptor signaling pathway / axonal growth cone / regulation of microtubule cytoskeleton organization / axon terminus / cellular response to forskolin / ephrin receptor binding / negative regulation of cell migration / protein tyrosine kinase binding / dendritic shaft / filopodium / caveola / regulation of actin cytoskeleton organization / adherens junction / postsynaptic density membrane / axon guidance / Schaffer collateral - CA1 synapse / neuromuscular junction / receptor protein-tyrosine kinase / negative regulation of ERK1 and ERK2 cascade / peptidyl-tyrosine phosphorylation / cellular response to amyloid-beta / positive regulation of peptidyl-tyrosine phosphorylation / negative regulation of neuron projection development / presynaptic membrane / kinase activity / nervous system development / amyloid-beta binding / early endosome membrane / perikaryon / protein tyrosine kinase activity / mitochondrial outer membrane / protein autophosphorylation / dendritic spine / protein stabilization / negative regulation of translation / cell adhesion / protein kinase activity / positive regulation of cell migration / positive regulation of protein phosphorylation / axon / external side of plasma membrane / glutamatergic synapse / dendrite / positive regulation of cell population proliferation Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Seiradake, E. / Schaupp, A. / del Toro Ruiz, D. / Kaufmann, R. / Mitakidis, N. / Harlos, K. / Aricescu, A.R. / Klein, R. / Jones, E.Y. | ||||||
![]() | ![]() Title: Structurally Encoded Intraclass Differences in Epha Clusters Drive Distinct Cell Responses Authors: Seiradake, E. / Schaupp, A. / Del Toro Ruiz, D. / Kaufmann, R. / Mitakidis, N. / Harlos, K. / Aricescu, A.R. / Klein, R. / Jones, E.Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.1 KB | Display | ![]() |
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PDB format | ![]() | 112.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.1 KB | Display | ![]() |
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Full document | ![]() | 473.6 KB | Display | |
Data in XML | ![]() | 27.2 KB | Display | |
Data in CIF | ![]() | 34.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bk4C ![]() 4bk5SC ![]() 4bkfC ![]() 4bkb C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 62649.336 Da / Num. of mol.: 1 / Fragment: HEPHA4 ECTODOMAIN, RESIDUES 20-547 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P54764, receptor protein-tyrosine kinase |
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#2: Protein | Mass: 20689.596 Da / Num. of mol.: 1 Fragment: HEPHRINA5 RECEPTOR BINDING DOMAIN, RESIDUES 27-166 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
Sequence details | CONTAINS ARTIFICIAL N-TERMINAL SECRETION SIGNAL AND C- TERMINAL POLY-HISTIDINE TAG CONTAINS ...CONTAINS ARTIFICIAL |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 9.05 Å3/Da / Density % sol: 85.3 % / Description: NONE |
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Crystal grow | Details: 0.01 M MGSO4, 1.8 M LISO4, 0.05 M SODIUM CACODYLATE PH 6 AND ADDITIVE 4% BENZAMIDINE-HCL |
-Data collection
Diffraction |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 4.95→48 Å / Num. obs: 11758 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 9.4 % / Rmerge(I) obs: 0.74 / Net I/σ(I): 3.32 | ||||||||||||||||||||
Reflection shell | Resolution: 4.95→5 Å / Redundancy: 7.6 % / Mean I/σ(I) obs: 0.32 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4BK5 Resolution: 5.3→84.87 Å / Cor.coef. Fo:Fc: 0.727 / Cor.coef. Fo:Fc free: 0.684 / SU B: 0.008 / SU ML: 0 / Cross valid method: THROUGHOUT / ESU R: 1.588 / ESU R Free: 1.688 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ONLY RIGID BODY AND TLS REFINEMENT WERE PERFORMED, NO INDIVIDUAL ATOM POSITIONS WERE REFINED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||
Displacement parameters | Biso mean: 243.358 Å2
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Refinement step | Cycle: LAST / Resolution: 5.3→84.87 Å
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LS refinement shell | Resolution: 5.3→5.438 Å / Total num. of bins used: 20
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