+Open data
-Basic information
Entry | Database: PDB / ID: 1g82 | |||||||||
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Title | STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 | |||||||||
Components | FIBROBLAST GROWTH FACTOR 9 | |||||||||
Keywords | HORMONE/GROWTH FACTOR / Fibroblast Growth Factor / HORMONE-GROWTH FACTOR COMPLEX | |||||||||
Function / homology | Function and homology information regulation of timing of cell differentiation / positive regulation of activin receptor signaling pathway / negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / positive regulation of reproductive process / Sertoli cell proliferation / Transcriptional regulation of testis differentiation / embryonic skeletal system development / FGFR3b ligand binding and activation / eye development / embryonic digestive tract development ...regulation of timing of cell differentiation / positive regulation of activin receptor signaling pathway / negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / positive regulation of reproductive process / Sertoli cell proliferation / Transcriptional regulation of testis differentiation / embryonic skeletal system development / FGFR3b ligand binding and activation / eye development / embryonic digestive tract development / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / mesenchymal cell proliferation / fibroblast growth factor receptor binding / FGFR2c ligand binding and activation / Activated point mutants of FGFR2 / Phospholipase C-mediated cascade; FGFR2 / FGFR4 ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / male sex determination / activin receptor signaling pathway / Signaling by activated point mutants of FGFR1 / FGFR1c ligand binding and activation / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 / lung-associated mesenchyme development / positive regulation of smoothened signaling pathway / positive regulation of vascular associated smooth muscle cell migration / positive regulation of vascular endothelial growth factor receptor signaling pathway / embryonic limb morphogenesis / positive regulation of mesenchymal cell proliferation / cardiac muscle cell proliferation / smoothened signaling pathway / inner ear morphogenesis / PI-3K cascade:FGFR3 / negative regulation of Wnt signaling pathway / PI-3K cascade:FGFR2 / positive regulation of stem cell proliferation / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / positive regulation of cell division / PI3K Cascade / fibroblast growth factor receptor signaling pathway / canonical Wnt signaling pathway / chondrocyte differentiation / SHC-mediated cascade:FGFR3 / vascular endothelial growth factor receptor signaling pathway / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR3 signaling / positive regulation of cardiac muscle cell proliferation / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / regulation of cell migration / FRS-mediated FGFR1 signaling / positive regulation of vascular associated smooth muscle cell proliferation / Signaling by FGFR2 in disease / substantia nigra development / Signaling by FGFR1 in disease / stem cell proliferation / positive regulation of epithelial cell proliferation / Negative regulation of FGFR3 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / animal organ morphogenesis / Negative regulation of FGFR1 signaling / growth factor activity / lung development / osteoblast differentiation / protein import into nucleus / Constitutive Signaling by Aberrant PI3K in Cancer / male gonad development / positive regulation of canonical Wnt signaling pathway / PIP3 activates AKT signaling / cell-cell signaling / heparin binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / angiogenesis / cell differentiation / positive regulation of protein phosphorylation / positive regulation of cell population proliferation / positive regulation of gene expression / negative regulation of transcription by RNA polymerase II / signal transduction / extracellular space / extracellular region / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | |||||||||
Authors | Hecht, H.J. / Adar, R. / Hofmann, B. / Bogin, O. / Weich, H. / Yayon, A. | |||||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces. Authors: Hecht, H.J. / Adar, R. / Hofmann, B. / Bogin, O. / Weich, H. / Yayon, A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g82.cif.gz | 148.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g82.ent.gz | 117.2 KB | Display | PDB format |
PDBx/mmJSON format | 1g82.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g82_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 1g82_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 1g82_validation.xml.gz | 32.5 KB | Display | |
Data in CIF | 1g82_validation.cif.gz | 43.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g8/1g82 ftp://data.pdbj.org/pub/pdb/validation_reports/g8/1g82 | HTTPS FTP |
-Related structure data
Related structure data | 2afgS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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Details | the biological assembly is a dimer. The asymmetric unit contains two dimers. The dimers are formed by molecule A and D, and B and C. |
-Components
#1: Protein | Mass: 18614.072 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PBACPAK9 / Cell line (production host): SF9 / Production host: unidentified baculovirus / References: PIR: A48137, UniProt: P31371*PLUS #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-SO4 / #4: Sugar | ChemComp-NAG / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 4.54 Å3/Da / Density % sol: 72.92 % | ||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 5.2 Details: Ammonium sulfate, MES, TRIS, pH 5.2, VAPOR DIFFUSION, SITTING DROP, temperature 292K | ||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.07 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Dec 22, 1998 / Details: mirrors |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→39.5 Å / Num. all: 40985 / Num. obs: 40985 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.3 % / Biso Wilson estimate: 68.211 Å2 / Rmerge(I) obs: 0.057 / Rsym value: 0.052 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 2.6→2.74 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.242 / Mean I/σ(I) obs: 3.3 / Num. unique all: 5971 / Rsym value: 0.222 / % possible all: 100 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 99.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 2AFG Resolution: 2.6→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 51.97 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→50 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / σ(F): 0 / % reflection Rfree: 5 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 2.7 |