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Open data
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Basic information
| Entry | Database: PDB / ID: 4o3u | ||||||
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| Title | Zymogen HGF-beta/MET with Zymogen Activator Peptide ZAP2.3 | ||||||
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Keywords | transferase/growth factor / trypsin homoloy / receptor activation / transferase-growth factor complex | ||||||
| Function / homology | Function and homology informationregulation of p38MAPK cascade / skeletal muscle cell proliferation / negative regulation of guanyl-nucleotide exchange factor activity / hepatocyte growth factor receptor activity / regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling / Drug-mediated inhibition of MET activation / MET activates STAT3 / negative regulation of hydrogen peroxide-mediated programmed cell death / MET Receptor Activation / MET interacts with TNS proteins ...regulation of p38MAPK cascade / skeletal muscle cell proliferation / negative regulation of guanyl-nucleotide exchange factor activity / hepatocyte growth factor receptor activity / regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling / Drug-mediated inhibition of MET activation / MET activates STAT3 / negative regulation of hydrogen peroxide-mediated programmed cell death / MET Receptor Activation / MET interacts with TNS proteins / endothelial cell morphogenesis / hepatocyte growth factor receptor signaling pathway / semaphorin receptor activity / MET receptor recycling / pancreas development / MET activates PTPN11 / MET activates RAP1 and RAC1 / Sema4D mediated inhibition of cell attachment and migration / MET activates PI3K/AKT signaling / positive regulation of endothelial cell chemotaxis / negative regulation of stress fiber assembly / MET activates PTK2 signaling / positive regulation of DNA biosynthetic process / cellular response to hepatocyte growth factor stimulus / branching morphogenesis of an epithelial tube / positive chemotaxis / negative regulation of Rho protein signal transduction / negative regulation of release of cytochrome c from mitochondria / chemoattractant activity / negative regulation of thrombin-activated receptor signaling pathway / semaphorin-plexin signaling pathway / negative regulation of interleukin-6 production / myoblast proliferation / positive regulation of interleukin-10 production / epithelial to mesenchymal transition / establishment of skin barrier / positive regulation of osteoblast differentiation / MET activates RAS signaling / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / MECP2 regulates neuronal receptors and channels / positive regulation of microtubule polymerization / Interleukin-7 signaling / negative regulation of autophagy / cell surface receptor protein tyrosine kinase signaling pathway / basal plasma membrane / platelet alpha granule lumen / molecular function activator activity / InlB-mediated entry of Listeria monocytogenes into host cell / epithelial cell proliferation / cell chemotaxis / excitatory postsynaptic potential / growth factor activity / liver development / Negative regulation of MET activity / receptor protein-tyrosine kinase / negative regulation of inflammatory response / cell morphogenesis / neuron differentiation / Constitutive Signaling by Aberrant PI3K in Cancer / Platelet degranulation / PIP3 activates AKT signaling / mitotic cell cycle / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / protein tyrosine kinase activity / Interleukin-4 and Interleukin-13 signaling / protein phosphatase binding / cell surface receptor signaling pathway / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / postsynapse / positive regulation of MAPK cascade / positive regulation of cell migration / signaling receptor binding / negative regulation of apoptotic process / cell surface / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)synthetic (others) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.04 Å | ||||||
Authors | Eigenbrot, C. / Landgraf, K.E. / Steffek, M. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2014Title: An allosteric switch for pro-HGF/Met signaling using zymogen activator peptides. Authors: Landgraf, K.E. / Steffek, M. / Quan, C. / Tom, J. / Yu, C. / Santell, L. / Maun, H.R. / Eigenbrot, C. / Lazarus, R.A. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 4o3u.cif.gz | 159 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4o3u.ent.gz | 122.8 KB | Display | PDB format |
| PDBx/mmJSON format | 4o3u.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4o3u_validation.pdf.gz | 446.8 KB | Display | wwPDB validaton report |
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| Full document | 4o3u_full_validation.pdf.gz | 457.9 KB | Display | |
| Data in XML | 4o3u_validation.xml.gz | 26.6 KB | Display | |
| Data in CIF | 4o3u_validation.cif.gz | 35.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o3/4o3u ftp://data.pdbj.org/pub/pdb/validation_reports/o3/4o3u | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4o3tC ![]() 1shyS S: Starting model for refinement C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 26800.920 Da / Num. of mol.: 1 / Fragment: HGF-beta (UNP Residues 25-567) / Mutation: V495G/C604S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HGF, HPTA / Production host: ![]() |
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| #2: Protein | Mass: 62714.141 Da / Num. of mol.: 1 / Fragment: Sema-PSI (UNP Residues 496-728) / Mutation: L303K/V304R/P305K/R306K/G307R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MET / Production host: ![]() References: UniProt: P08581, receptor protein-tyrosine kinase |
| #3: Protein/peptide | Mass: 1786.081 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic peptide library displayed on phage / Source: (synth.) synthetic (others) |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.44 Å3/Da / Density % sol: 64.26 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 8% PEG8000, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
| Diffraction | Mean temperature: 110 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9794 Å |
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: May 23, 2012 |
| Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
| Reflection | Resolution: 3.04→34.76 Å / Num. all: 24419 / Num. obs: 24340 / % possible obs: 97.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.6 % / Biso Wilson estimate: 102.77 Å2 / Rsym value: 0.056 / Net I/σ(I): 23 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1SHY Resolution: 3.04→34.76 Å / Cor.coef. Fo:Fc: 0.8969 / Cor.coef. Fo:Fc free: 0.8574 / SU R Cruickshank DPI: 1.39 / Isotropic thermal model: individual atom isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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| Displacement parameters | Biso mean: 94.12 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.593 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.04→34.76 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 3.04→3.17 Å / Total num. of bins used: 12
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Homo sapiens (human)
X-RAY DIFFRACTION
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