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Yorodumi- PDB-1afc: STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE ... -
+Open data
-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 | |||||||||
Components | ACIDIC FIBROBLAST GROWTH FACTOR | |||||||||
Keywords | GROWTH FACTOR | |||||||||
Function / homology | Function and homology information 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 / PI-3K cascade:FGFR1 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / PI3K Cascade / PIP3 activates AKT signaling / RAF/MAP kinase cascade / 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 / regulation of cell migration / positive regulation of endothelial cell migration / animal organ morphogenesis / growth factor activity / positive regulation of angiogenesis / integrin binding / heparin binding / cell cortex / cellular response to heat / 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 / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | |||||||||
Authors | Zhu, X. / Hsu, B.T. / Rees, D.C. | |||||||||
Citation | Journal: Structure / Year: 1993 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: Journal: Science / Year: 1991 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1afc.cif.gz | 216.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1afc.ent.gz | 171 KB | Display | PDB format |
PDBx/mmJSON format | 1afc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1afc_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 1afc_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 1afc_validation.xml.gz | 41.8 KB | Display | |
Data in CIF | 1afc_validation.cif.gz | 59.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/af/1afc ftp://data.pdbj.org/pub/pdb/validation_reports/af/1afc | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
-Components
#1: Protein | Mass: 15871.007 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Production host: Escherichia coli (E. coli) / References: UniProt: P03968 #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: X-RAY DIFFRACTION |
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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 |
-Processing
Software |
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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 |