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Yorodumi- PDB-2afg: 2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR -
+Open data
-Basic information
Entry | Database: PDB / ID: 2afg | |||||||||
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Title | 2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR | |||||||||
Components | ACIDIC FIBROBLAST GROWTH FACTOR | |||||||||
Keywords | GROWTH FACTOR | |||||||||
Function / homology | Function and homology information mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / FGFR3b ligand binding and activation / 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 / FGFR2b ligand binding and activation / positive regulation of cholesterol biosynthetic process ...mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / FGFR3b ligand binding and activation / 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 / FGFR2b ligand binding and activation / positive regulation of cholesterol biosynthetic process / 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 / FGFR1b ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / Signaling by activated point mutants of FGFR1 / FGFR1c ligand binding and activation / organ induction / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 / positive regulation of hepatocyte proliferation / S100 protein binding / positive regulation of intracellular signal transduction / Signaling by FGFR2 IIIa TM / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / positive regulation of sprouting angiogenesis / PI-3K cascade:FGFR1 / positive regulation of cell division / PI3K Cascade / anatomical structure morphogenesis / 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 / Signaling by FGFR3 in disease / FRS-mediated FGFR4 signaling / epithelial cell proliferation / FRS-mediated FGFR1 signaling / Signaling by FGFR2 in disease / Hsp70 protein binding / Signaling by FGFR1 in disease / regulation of cell migration / activation of protein kinase B activity / positive regulation of endothelial cell migration / extracellular matrix / lung development / positive regulation of MAP kinase activity / Negative regulation of FGFR3 signaling / animal organ morphogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Negative regulation of FGFR1 signaling / growth factor activity / wound healing / Constitutive Signaling by Aberrant PI3K in Cancer / integrin binding / positive regulation of angiogenesis / PIP3 activates AKT signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / heparin binding / RAF/MAP kinase cascade / 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 / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | |||||||||
Authors | Blaber, M. / Disalvo, J. / Thomas, K.A. | |||||||||
Citation | Journal: Biochemistry / Year: 1996 Title: X-ray crystal structure of human acidic fibroblast growth factor. Authors: Blaber, M. / DiSalvo, J. / Thomas, K.A. #1: Journal: Protein Sci. / Year: 1993 Title: Refinement of the Structure of Human Basic Fibroblast Growth Factor at 1.6 Angstroms Resolution and Analysis of Presumed Heparin Binding Sites by Selenate Substitution Authors: Eriksson, A.E. / Cousens, L.S. / Matthews, B.W. #2: 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 | 2afg.cif.gz | 109.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2afg.ent.gz | 86.8 KB | Display | PDB format |
PDBx/mmJSON format | 2afg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2afg_validation.pdf.gz | 407.4 KB | Display | wwPDB validaton report |
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Full document | 2afg_full_validation.pdf.gz | 430.7 KB | Display | |
Data in XML | 2afg_validation.xml.gz | 13.8 KB | Display | |
Data in CIF | 2afg_validation.cif.gz | 21 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/af/2afg ftp://data.pdbj.org/pub/pdb/validation_reports/af/2afg | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.999696, -0.024494, -0.002713), Vector: |
-Components
#1: Protein | Mass: 15857.864 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P05230 #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.13 % |
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Conc.: 9-11 % / Common name: PEG |
-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 19981 / % possible obs: 55 % / Rmerge(I) obs: 0.041 |
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-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→20 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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