+Open data
-Basic information
Entry | Database: PDB / ID: 3ch8 | ||||||
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Title | The crystal structure of PDZ-Fibronectin fusion protein | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / fibronectin / PDZ | ||||||
Function / homology | Function and homology information basal protein localization / ErbB-2 class receptor binding / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / hemidesmosome / postsynaptic specialization / negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / Fibronectin matrix formation / Extracellular matrix organization ...basal protein localization / ErbB-2 class receptor binding / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / hemidesmosome / postsynaptic specialization / negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / Fibronectin matrix formation / Extracellular matrix organization / positive regulation of substrate-dependent cell migration, cell attachment to substrate / intermediate filament cytoskeleton organization / neural crest cell migration involved in autonomic nervous system development / peptidase activator activity / fibrinogen complex / peptide cross-linking / integrin activation / negative regulation of monocyte chemotactic protein-1 production / ALK mutants bind TKIs / cell-substrate junction assembly / establishment or maintenance of epithelial cell apical/basal polarity / biological process involved in interaction with symbiont / Molecules associated with elastic fibres / proteoglycan binding / extracellular matrix structural constituent / MET activates PTK2 signaling / Syndecan interactions / RHOB GTPase cycle / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / negative regulation of NF-kappaB transcription factor activity / p130Cas linkage to MAPK signaling for integrins / RHOC GTPase cycle / endodermal cell differentiation / regulation of postsynaptic membrane neurotransmitter receptor levels / GRB2:SOS provides linkage to MAPK signaling for Integrins / response to muramyl dipeptide / Signaling by ALK fusions and activated point mutants / RHOG GTPase cycle / Non-integrin membrane-ECM interactions / basement membrane / endoplasmic reticulum-Golgi intermediate compartment / ECM proteoglycans / RHOA GTPase cycle / protein targeting / RAC2 GTPase cycle / RAC3 GTPase cycle / positive regulation of axon extension / Integrin cell surface interactions / Nuclear events stimulated by ALK signaling in cancer / Signaling by ERBB2 / RAC1 GTPase cycle / collagen binding / Degradation of the extracellular matrix / Integrin signaling / substrate adhesion-dependent cell spreading / Constitutive Signaling by Overexpressed ERBB2 / extracellular matrix / basal plasma membrane / cell-matrix adhesion / regulation of ERK1 and ERK2 cascade / platelet alpha granule lumen / integrin-mediated signaling pathway / acute-phase response / Cell surface interactions at the vascular wall / Post-translational protein phosphorylation / Signaling by ERBB2 TMD/JMD mutants / regulation of protein phosphorylation / Signaling by high-kinase activity BRAF mutants / neuromuscular junction / MAP2K and MAPK activation / wound healing / Signaling by ERBB2 ECD mutants / epidermal growth factor receptor signaling pathway / Signaling by ERBB2 KD Mutants / structural constituent of cytoskeleton / Downregulation of ERBB2 signaling / response to wounding / GPER1 signaling / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of fibroblast proliferation / Signaling by BRAF and RAF1 fusions / integrin binding / Platelet degranulation / cell junction / heparin binding / nervous system development / cellular response to tumor necrosis factor Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Makabe, K. / Huang, J. / Koide, A. / Koide, S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2009 Title: Structural basis for exquisite specificity of affinity clamps, synthetic binding proteins generated through directed domain-interface evolution. Authors: Huang, J. / Makabe, K. / Biancalana, M. / Koide, A. / Koide, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ch8.cif.gz | 52.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ch8.ent.gz | 38 KB | Display | PDB format |
PDBx/mmJSON format | 3ch8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ch/3ch8 ftp://data.pdbj.org/pub/pdb/validation_reports/ch/3ch8 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20996.334 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: see REMARK 400,see REMARK 400 / Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET system / Gene: FN1, FN / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P02751, UniProt: Q96RT1*PLUS |
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#2: Protein/peptide | Mass: 927.011 Da / Num. of mol.: 1 / Fragment: C-terminal residues / Source method: obtained synthetically / Source: (synth.) Synthetic construct (others) |
#3: Chemical | ChemComp-MG / |
#4: Water | ChemComp-HOH / |
Compound details | THIS PROTEIN IS A VARIANT OF PREVIOUSLY DEPOSITED FUSION PROTEIN (PDBID: 2QBW). THE CIRCULAR ...THIS PROTEIN IS A VARIANT OF PREVIOUSLY |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 31% isopropanol, 0.1M HEPES, 0.2M MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 16, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. all: 23031 / Num. obs: 23031 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 23.74 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.512 / Mean I/σ(I) obs: 2.712 / Num. unique all: 2256 / % possible all: 97 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→20 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.938 / SU B: 11.257 / SU ML: 0.164 / Cross valid method: THROUGHOUT / ESU R: 0.146 / ESU R Free: 0.152 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.924 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.949 Å / Total num. of bins used: 20
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