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Yorodumi- PDB-1jtc: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jtc | ||||||
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Title | Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE (L44F) | ||||||
Components | acidic fibroblast growth factor | ||||||
Keywords | HORMONE/GROWTH FACTOR / beta-trefoil / HORMONE-GROWTH FACTOR COMPLEX | ||||||
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 / positive regulation of sprouting angiogenesis / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / positive regulation of cell division / PI3K Cascade / fibroblast growth factor receptor signaling pathway / anatomical structure morphogenesis / 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 / Signaling by FGFR3 in disease / FRS-mediated FGFR1 signaling / Signaling by FGFR2 in disease / Hsp70 protein binding / Signaling by FGFR1 in disease / activation of protein kinase B activity / positive regulation of endothelial cell migration / extracellular matrix / epithelial 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 / positive regulation of MAP kinase activity / lung development / wound healing / positive regulation of angiogenesis / Constitutive Signaling by Aberrant PI3K in Cancer / integrin binding / PIP3 activates AKT signaling / heparin binding / cellular response to heat / cell cortex / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / 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 / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Brych, S.R. / Blaber, S.I. / Logan, T.M. / Blaber, M. | ||||||
Citation | Journal: Protein Sci. / Year: 2001 Title: Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil. Authors: Brych, S.R. / Blaber, S.I. / Logan, T.M. / Blaber, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jtc.cif.gz | 133.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jtc.ent.gz | 103 KB | Display | PDB format |
PDBx/mmJSON format | 1jtc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jtc_validation.pdf.gz | 423 KB | Display | wwPDB validaton report |
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Full document | 1jtc_full_validation.pdf.gz | 434.7 KB | Display | |
Data in XML | 1jtc_validation.xml.gz | 13.6 KB | Display | |
Data in CIF | 1jtc_validation.cif.gz | 23.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/1jtc ftp://data.pdbj.org/pub/pdb/validation_reports/jt/1jtc | HTTPS FTP |
-Related structure data
Related structure data | 1jqzSC 1jt3C 1jt4C 1jt5C 1jt7C S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 16720.764 Da / Num. of mol.: 4 / Mutation: L44F 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-FMT / #3: 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: 2.96 Å3/Da / Density % sol: 57.82 % | ||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: sodium formate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 or 10 ℃ | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jul 10, 2000 / Details: Osmic Blue confocal mirrors |
Radiation | Monochromator: Osmic Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→36.9 Å / Num. all: 85721 / Num. obs: 85721 / % possible obs: 88.2 % / Observed criterion σ(F): 2.6 / Observed criterion σ(I): 2.6 / Redundancy: 1.2 % / Biso Wilson estimate: 11.3 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 26.5 |
Reflection shell | Resolution: 1.7→1.74 Å / Rmerge(I) obs: 0.319 / Mean I/σ(I) obs: 2.6 / % possible all: 69.1 |
Reflection | *PLUS Num. obs: 72647 / % possible obs: 88.1 % / Num. measured all: 274969 |
Reflection shell | *PLUS % possible obs: 64.8 % / Mean I/σ(I) obs: 2.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1JQZ Resolution: 1.7→36.9 Å / Isotropic thermal model: TRONRUD / Stereochemistry target values: TRONRUD
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Solvent computation | Solvent model: TNT / Bsol: 248.83 Å2 / ksol: 0.977 e/Å3 | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→36.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.73 Å /
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Num. reflection Rfree: 7195 / % reflection Rfree: 10 % / Rfactor all: 0.197 / Rfactor obs: 0.193 / Rfactor Rfree: 0.239 / Rfactor Rwork: 0.193 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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