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Open data
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Basic information
Entry | Database: PDB / ID: 1ijt | ||||||
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Title | Crystal Structure of Fibroblast Growth Factor 4 (FGF4) | ||||||
![]() | fibroblast growth factor 4 | ||||||
![]() | HORMONE/GROWTH FACTOR / b-trefoil fold / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | ![]() FGFR3 mutant receptor activation / cranial suture morphogenesis / : / FGFRL1 modulation of FGFR1 signaling / chondroblast differentiation / apoptotic process involved in morphogenesis / regulation of endothelial cell chemotaxis to fibroblast growth factor / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 ...FGFR3 mutant receptor activation / cranial suture morphogenesis / : / FGFRL1 modulation of FGFR1 signaling / chondroblast differentiation / apoptotic process involved in morphogenesis / regulation of endothelial cell chemotaxis to fibroblast growth factor / 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 / Signaling by activated point mutants of FGFR1 / FGFR1c ligand binding and activation / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 / embryonic hindlimb morphogenesis / cartilage condensation / stem cell population maintenance / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / odontogenesis of dentin-containing tooth / positive regulation of cell division / PI3K Cascade / fibroblast growth factor receptor signaling pathway / SHC-mediated cascade:FGFR3 / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR3 signaling / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / FRS-mediated FGFR1 signaling / Signaling by FGFR2 in disease / Signaling by FGFR1 in disease / cellular response to leukemia inhibitory factor / Negative regulation of FGFR3 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Negative regulation of FGFR1 signaling / growth factor activity / Constitutive Signaling by Aberrant PI3K in Cancer / MAPK cascade / PIP3 activates AKT signaling / cell-cell signaling / heparin binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of ERK1 and ERK2 cascade / positive regulation of cell population proliferation / negative regulation of apoptotic process / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bellosta, P. / Plotnikov, A.N. / Eliseenkova, A.V. / Basilico, C. / Mohammadi, M. | ||||||
![]() | ![]() Title: Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis. Authors: Bellosta, P. / Iwahori, A. / Plotnikov, A.N. / Eliseenkova, A.V. / Basilico, C. / Mohammadi, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.8 KB | Display | ![]() |
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PDB format | ![]() | 26.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 372.6 KB | Display | ![]() |
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Full document | ![]() | 373.7 KB | Display | |
Data in XML | ![]() | 4 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2fgfS S: Starting model for refinement |
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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: 14270.591 Da / Num. of mol.: 1 / Fragment: b-trefoil domain / Mutation: S182G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.93 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 8000, ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 43 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 15, 1998 |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→25 Å / Num. all: 40562 / Num. obs: 40562 / % possible obs: 99.6 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 16.5 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.109 / % possible all: 99.5 |
Reflection | *PLUS Num. obs: 11590 / Num. measured all: 40562 |
Reflection shell | *PLUS % possible obs: 99.5 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2FGF Resolution: 1.8→25 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: CNS / Bsol: 74.852 Å2 / ksol: 0.571 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→25 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / σ(F): 0 / % reflection Rfree: 5.1 % / Rfactor obs: 0.194 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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