+Open data
-Basic information
Entry | Database: PDB / ID: 1bff | ||||||
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Title | THE 154 AMINO ACID FORM OF HUMAN BASIC FIBROBLAST GROWTH FACTOR | ||||||
Components | BASIC FIBROBLAST GROWTH FACTOR | ||||||
Keywords | GROWTH FACTOR | ||||||
Function / homology | Function and homology information growth factor dependent regulation of skeletal muscle satellite cell proliferation / positive regulation of inner ear auditory receptor cell differentiation / positive regulation of neuroepithelial cell differentiation / regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of lens fiber cell differentiation / positive regulation of cell fate specification / regulation of retinal cell programmed cell death / Formation of intermediate mesoderm / regulation of cell migration involved in sprouting angiogenesis / FGFRL1 modulation of FGFR1 signaling ...growth factor dependent regulation of skeletal muscle satellite cell proliferation / positive regulation of inner ear auditory receptor cell differentiation / positive regulation of neuroepithelial cell differentiation / regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of lens fiber cell differentiation / positive regulation of cell fate specification / regulation of retinal cell programmed cell death / Formation of intermediate mesoderm / regulation of cell migration involved in sprouting angiogenesis / FGFRL1 modulation of FGFR1 signaling / corticotropin hormone secreting cell differentiation / thyroid-stimulating hormone-secreting cell differentiation / chondroblast differentiation / lymphatic endothelial cell migration / chemokine binding / negative regulation of fibroblast growth factor receptor signaling pathway / POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / positive regulation of cerebellar granule cell precursor proliferation / positive regulation of endothelial cell chemotaxis to fibroblast growth factor / cerebellar granule cell precursor proliferation / receptor-receptor interaction / positive regulation of stem cell differentiation / hyaluronan catabolic process / glial cell differentiation / regulation of endothelial cell chemotaxis to fibroblast growth factor / inner ear auditory receptor cell differentiation / negative regulation of wound healing / stem cell development / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / embryonic morphogenesis / FGFR2b ligand binding and activation / fibroblast growth factor receptor binding / angiogenesis involved in coronary vascular morphogenesis / FGFR2c ligand binding and activation / Activated point mutants of FGFR2 / positive regulation of epithelial tube formation / Phospholipase C-mediated cascade; FGFR2 / FGFR4 ligand binding and activation / FGFR1b ligand binding and activation / mammary gland epithelial cell differentiation / 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 / paracrine signaling / negative regulation of fibroblast migration / positive regulation of endothelial cell chemotaxis / endothelial cell proliferation / cell migration involved in sprouting angiogenesis / embryo development ending in birth or egg hatching / positive regulation of vascular endothelial cell proliferation / Signaling by FGFR2 IIIa TM / branching involved in ureteric bud morphogenesis / positive regulation of DNA biosynthetic process / Syndecan interactions / positive regulation of neuroblast proliferation / positive regulation of cell migration involved in sprouting angiogenesis / PI-3K cascade:FGFR3 / positive regulation of stem cell proliferation / PI-3K cascade:FGFR2 / positive regulation of sprouting angiogenesis / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / chemoattractant activity / negative regulation of blood vessel endothelial cell migration / canonical Wnt signaling pathway / positive regulation of cell division / Non-integrin membrane-ECM interactions / neuroblast proliferation / PI3K Cascade / response to axon injury / positive regulation of blood vessel endothelial cell migration / fibroblast growth factor receptor signaling pathway / positive regulation of osteoblast differentiation / regulation of angiogenesis / SHC-mediated cascade:FGFR3 / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / negative regulation of stem cell proliferation / release of sequestered calcium ion into cytosol / FRS-mediated FGFR3 signaling / FRS-mediated FGFR2 signaling / positive regulation of cardiac muscle cell proliferation / Signaling by FGFR3 in disease / FRS-mediated FGFR4 signaling / ERK1 and ERK2 cascade / FRS-mediated FGFR1 signaling / positive regulation of vascular associated smooth muscle cell proliferation / Signaling by FGFR2 in disease / substantia nigra development / Signaling by FGFR1 in disease / positive regulation of endothelial cell proliferation / positive regulation of endothelial cell migration / nuclear receptor coactivator activity / phosphatidylinositol 3-kinase/protein kinase B signal transduction Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2 Å | ||||||
Authors | Kastrup, J.S. / Eriksson, E.S. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1997 Title: X-ray structure of the 154-amino-acid form of recombinant human basic fibroblast growth factor. comparison with the truncated 146-amino-acid form. Authors: Kastrup, J.S. / Eriksson, E.S. / Dalboge, H. / Flodgaard, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bff.cif.gz | 36.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bff.ent.gz | 26.9 KB | Display | PDB format |
PDBx/mmJSON format | 1bff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bf/1bff ftp://data.pdbj.org/pub/pdb/validation_reports/bf/1bff | HTTPS FTP |
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-Related structure data
Related structure data | 4fgfS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14800.098 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PHD329 / Production host: Escherichia coli (E. coli) / Strain (production host): MC1061 / References: UniProt: P09038 |
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#2: Chemical | ChemComp-PO4 / |
#3: Chemical | ChemComp-BME / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: THE PROTEIN WAS CRYSTALLIZED FROM 30-40 % PEG1000 AND 0.2-0.3 % 2-MERCAPTOETHANOL BY THE HANGING DROP VAPOR DIFFUSION METHOD., pH 7.5, vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Jul 1, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. obs: 7035 / % possible obs: 84 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 22 Å2 / Rsym value: 0.047 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 1.2 % / Mean I/σ(I) obs: 2.1 / Rsym value: 0.201 / % possible all: 46 |
Reflection | *PLUS Num. measured all: 15506 / Rmerge(I) obs: 0.043 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 4FGF Resolution: 2→20 Å / σ(F): 0 / Stereochemistry target values: TNT PROTGEO Details: THE B-FACTORS WERE REFINED USING PROLSQ. THERE IS ONE RESIDUE (SER 151) WITH DEVIATING PHI, PSI ANGLES IN THE RAMACHANDRAN PLOT.
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.19 / Rfactor Rwork: 0.19 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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