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- PDB-1afc: STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1afc | |||||||||
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Title | STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR | |||||||||
![]() | ACIDIC FIBROBLAST GROWTH FACTOR | |||||||||
![]() | GROWTH FACTOR | |||||||||
Function / homology | ![]() FGFR4 ligand binding and activation / FGFR1b ligand binding and activation / FGFR3b ligand binding and activation / FGFR3c ligand binding and activation / FGFR1c ligand binding and activation / FGFR2c ligand binding and activation / FGFR2b ligand binding and activation / Phospholipase C-mediated cascade: FGFR1 / Phospholipase C-mediated cascade; FGFR2 / Phospholipase C-mediated cascade; FGFR3 ...FGFR4 ligand binding and activation / FGFR1b ligand binding and activation / FGFR3b ligand binding and activation / FGFR3c ligand binding and activation / FGFR1c ligand binding and activation / FGFR2c ligand binding and activation / FGFR2b ligand binding and activation / Phospholipase C-mediated cascade: FGFR1 / Phospholipase C-mediated cascade; FGFR2 / Phospholipase C-mediated cascade; FGFR3 / Phospholipase C-mediated cascade; FGFR4 / Downstream signaling of activated FGFR1 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR1 signaling / SHC-mediated cascade:FGFR2 / FRS-mediated FGFR2 signaling / SHC-mediated cascade:FGFR3 / FRS-mediated FGFR3 signaling / FRS-mediated FGFR4 signaling / SHC-mediated cascade:FGFR4 / RAF/MAP kinase cascade / PI-3K cascade:FGFR1 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / PI3K Cascade / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Negative regulation of FGFR1 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / positive regulation of cholesterol biosynthetic process / fibroblast growth factor receptor binding / S100 protein binding / positive regulation of intracellular signal transduction / positive regulation of sprouting angiogenesis / positive regulation of cell division / fibroblast growth factor receptor signaling pathway / activation of protein kinase B activity / positive regulation of endothelial cell migration / positive regulation of epithelial cell proliferation / animal organ morphogenesis / growth factor activity / lung development / wound healing / positive regulation of angiogenesis / integrin binding / heparin binding / cellular response to heat / cell cortex / angiogenesis / positive regulation of ERK1 and ERK2 cascade / cell differentiation / positive regulation of cell migration / positive regulation of cell population proliferation / positive regulation of gene expression / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Zhu, X. / Hsu, B.T. / Rees, D.C. | |||||||||
![]() | ![]() Title: Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor. Authors: Zhu, X. / Hsu, B.T. / Rees, D.C. #1: ![]() Title: Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors Authors: Zhu, X. / Komiya, H. / Chirino, A. / Faham, S. / Fox, G.M. / Arakawa, T. / Hsu, B.T. / Rees, D.C. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 216.3 KB | Display | ![]() |
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PDB format | ![]() | 171 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 41.8 KB | Display | |
Data in CIF | ![]() | 59.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
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Components
#1: Protein | Mass: 15871.007 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Polysaccharide | 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose / sucrose octasulfate |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.61 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.7 Å / Num. obs: 31326 / % possible obs: 95 % / Num. measured all: 138212 / Rmerge(I) obs: 0.118 |
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Processing
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Refinement | Rfactor Rwork: 0.204 / Rfactor obs: 0.204 / Highest resolution: 2.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.7 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.7 Å / Rfactor obs: 0.204 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.7 |