|Entry||Database: PDB / ID: 2g4m|
|Title||Insulin collected at 2.0 A wavelength|
|Keywords||HORMONE/GROWTH FACTOR / insulin at 2.0 A wavelength / HORMONE-GROWTH FACTOR COMPLEX|
|Function / homology|
Function and homology information
glycoprotein biosynthetic process / lactate biosynthetic process / positive regulation of lipoprotein lipase activity / positive regulation of fatty acid biosynthetic process / response to L-arginine / lipoprotein biosynthetic process / positive regulation of glucose metabolic process / lipid biosynthetic process / alpha-beta T cell activation / negative regulation of glycogen catabolic process ...glycoprotein biosynthetic process / lactate biosynthetic process / positive regulation of lipoprotein lipase activity / positive regulation of fatty acid biosynthetic process / response to L-arginine / lipoprotein biosynthetic process / positive regulation of glucose metabolic process / lipid biosynthetic process / alpha-beta T cell activation / negative regulation of glycogen catabolic process / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / positive regulation of respiratory burst / negative regulation of respiratory burst involved in inflammatory response / negative regulation of gluconeogenesis / regulation of cellular amino acid metabolic process / negative regulation of acute inflammatory response / negative regulation of reactive oxygen species biosynthetic process / regulation of protein localization to plasma membrane / positive regulation of dendritic spine maintenance / positive regulation of glycogen biosynthetic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of protein secretion / negative regulation of lipid catabolic process / fatty acid homeostasis / positive regulation of insulin receptor signaling pathway / neuron projection maintenance / insulin-like growth factor receptor binding / positive regulation of DNA replication / positive regulation of protein autophosphorylation / positive regulation of glycolytic process / regulation of transmembrane transporter activity / positive regulation of mitotic nuclear division / positive regulation of cytokine production / acute-phase response / activation of protein kinase B activity / positive regulation of glucose import / hormone activity / negative regulation of proteolysis / negative regulation of protein catabolic process / insulin receptor binding / positive regulation of protein localization to nucleus / insulin receptor signaling pathway / vasodilation / glucose metabolic process / glucose homeostasis / wound healing / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase signaling / protease binding / positive regulation of NF-kappaB transcription factor activity / positive regulation of protein kinase B signaling / positive regulation of cell migration / G protein-coupled receptor signaling pathway / positive regulation of cell population proliferation / extracellular space / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin-like superfamily / Insulin family signature.
Similarity search - Domain/homology
|Biological species||Sus scrofa (pig)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.8 Å|
|Authors||Mueller-Dieckmann, C. / Weiss, M.S.|
|Citation||Journal: Acta Crystallogr.,Sect.D / Year: 2007|
Title: On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.
Authors: Mueller-Dieckmann, C. / Panjikar, S. / Schmidt, A. / Mueller, S. / Kuper, J. / Geerlof, A. / Wilmanns, M. / Singh, R.K. / Tucker, P.A. / Weiss, M.S.
|Structure viewer||Molecule: |
Downloads & links
A: Insulin A chain
B: Insulin B chain
A: Insulin A chain
B: Insulin B chain
A: Insulin A chain
B: Insulin B chain
|Components on special symmetry positions|
|#1: Protein/peptide|| |
Mass: 2383.698 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P01315
|#2: Protein/peptide|| |
Mass: 3403.927 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / References: UniProt: P01315
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 3.45 Å3/Da / Density % sol: 64.36 %|
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: EMBL/DESY, Hamburg / Beamline: X12 / Wavelength: 2 Å|
|Detector||Type: MARRESEARCH / Detector: CCD / Date: Jan 1, 2005|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 2 Å / Relative weight: 1|
|Reflection||Resolution: 1.8→30 Å / Num. obs: 7537 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0|
|Refinement||Method to determine structure: FOURIER SYNTHESIS / Resolution: 1.8→30 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.928 / SU B: 4.756 / SU ML: 0.069 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.089 / ESU R Free: 0.102 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS|
|Solvent computation||Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK|
|Displacement parameters||Biso mean: 25.011 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.8→30 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 1.8→1.847 Å / Total num. of bins used: 20 |
|Refinement TLS params.||Method: refined / Origin x: 20.4067 Å / Origin y: 38.7807 Å / Origin z: 28.4551 Å|
|Refinement TLS group|
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