+Open data
-Basic information
Entry | Database: PDB / ID: 2p23 | ||||||
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Title | Crystal structure of human FGF19 | ||||||
Components | Fibroblast growth factor 19 | ||||||
Keywords | SIGNALING PROTEIN / atypical beta-trefoil fold | ||||||
Function / homology | Function and homology information negative regulation of bile acid biosynthetic process / betaKlotho-mediated ligand binding / fibroblast growth factor receptor binding / FGFR4 ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / PI-3K cascade:FGFR4 / PI3K Cascade / fibroblast growth factor receptor signaling pathway / SHC-mediated cascade:FGFR4 / FRS-mediated FGFR4 signaling ...negative regulation of bile acid biosynthetic process / betaKlotho-mediated ligand binding / fibroblast growth factor receptor binding / FGFR4 ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / PI-3K cascade:FGFR4 / PI3K Cascade / fibroblast growth factor receptor signaling pathway / SHC-mediated cascade:FGFR4 / FRS-mediated FGFR4 signaling / regulation of cell migration / positive regulation of glucose import / Negative regulation of FGFR4 signaling / animal organ morphogenesis / positive regulation of JNK cascade / growth factor activity / Constitutive Signaling by Aberrant PI3K in Cancer / PIP3 activates AKT signaling / nervous system development / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / cell differentiation / positive regulation of ERK1 and ERK2 cascade / positive regulation of protein phosphorylation / negative regulation of gene expression / positive regulation of cell population proliferation / positive regulation of gene expression / extracellular space / extracellular region / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Mohammadi, M. | ||||||
Citation | Journal: Mol.Cell.Biol. / Year: 2007 Title: Molecular insights into the klotho-dependent, endocrine mode of action of fibroblast growth factor 19 subfamily members. Authors: Goetz, R. / Beenken, A. / Ibrahimi, O.A. / Kalinina, J. / Olsen, S.K. / Eliseenkova, A.V. / Xu, C. / Neubert, T.A. / Zhang, F. / Linhardt, R.J. / Yu, X. / White, K.E. / Inagaki, T. / ...Authors: Goetz, R. / Beenken, A. / Ibrahimi, O.A. / Kalinina, J. / Olsen, S.K. / Eliseenkova, A.V. / Xu, C. / Neubert, T.A. / Zhang, F. / Linhardt, R.J. / Yu, X. / White, K.E. / Inagaki, T. / Kliewer, S.A. / Yamamoto, M. / Kurosu, H. / Ogawa, Y. / Kuro-O, M. / Lanske, B. / Razzaque, M.S. / Mohammadi, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2p23.cif.gz | 67.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2p23.ent.gz | 47.7 KB | Display | PDB format |
PDBx/mmJSON format | 2p23.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2p23_validation.pdf.gz | 436.1 KB | Display | wwPDB validaton report |
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Full document | 2p23_full_validation.pdf.gz | 439 KB | Display | |
Data in XML | 2p23_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | 2p23_validation.cif.gz | 15.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p2/2p23 ftp://data.pdbj.org/pub/pdb/validation_reports/p2/2p23 | HTTPS FTP |
-Related structure data
Related structure data | 2p39C 1pwaS 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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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 21713.748 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FGF19 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) pLys-S / References: UniProt: O95750 #2: 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 grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.75 Details: 100 mM tri-sodium citrate, 14% PEG 1000, pH 5.75, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.97928 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 27, 2005 |
Radiation | Monochromator: KOHZU DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97928 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. all: 25585 / Num. obs: 25585 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Rsym value: 0.05 / Net I/σ(I): 25.6 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 4 % / Num. unique all: 2564 / Rsym value: 0.34 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1PWA Resolution: 1.8→25 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→25 Å
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Refine LS restraints |
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