+Open data
-Basic information
Entry | Database: PDB / ID: 1g7a | ||||||
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Title | 1.2 A structure of T3R3 human insulin at 100 K | ||||||
Components |
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Keywords | hormone/growth factor / T3R3 Insulin Hexamer / hormone-growth factor COMPLEX | ||||||
Function / homology | Function and homology information negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of peptide hormone secretion ...negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / negative regulation of acute inflammatory response / Regulation of gene expression in beta cells / alpha-beta T cell activation / regulation of cellular amino acid metabolic process / negative regulation of respiratory burst involved in inflammatory response / positive regulation of dendritic spine maintenance / positive regulation of glycogen biosynthetic process / Synthesis, secretion, and deacylation of Ghrelin / negative regulation of protein secretion / regulation of protein localization to plasma membrane / fatty acid homeostasis / Signal attenuation / negative regulation of lipid catabolic process / negative regulation of gluconeogenesis / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / COPI-mediated anterograde transport / positive regulation of lipid biosynthetic process / negative regulation of reactive oxygen species biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of insulin receptor signaling pathway / nitric oxide-cGMP-mediated signaling / transport vesicle / positive regulation of protein autophosphorylation / Insulin receptor recycling / insulin-like growth factor receptor binding / neuron projection maintenance / NPAS4 regulates expression of target genes / positive regulation of protein metabolic process / positive regulation of brown fat cell differentiation / activation of protein kinase B activity / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of glycolytic process / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / positive regulation of nitric-oxide synthase activity / positive regulation of cytokine production / positive regulation of long-term synaptic potentiation / acute-phase response / Regulation of insulin secretion / negative regulation of protein catabolic process / endosome lumen / positive regulation of glucose import / positive regulation of protein secretion / negative regulation of proteolysis / positive regulation of cell differentiation / regulation of transmembrane transporter activity / insulin receptor binding / wound healing / regulation of synaptic plasticity / vasodilation / hormone activity / cognition / positive regulation of neuron projection development / positive regulation of protein localization to nucleus / Golgi lumen / glucose metabolic process / regulation of protein localization / glucose homeostasis / insulin receptor signaling pathway / cell-cell signaling / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of NF-kappaB transcription factor activity / positive regulation of cell growth / protease binding / secretory granule lumen / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cell migration / G protein-coupled receptor signaling pathway / Amyloid fiber formation / Golgi membrane / endoplasmic reticulum lumen / negative regulation of gene expression / positive regulation of cell population proliferation / positive regulation of gene expression / regulation of DNA-templated transcription / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.2 Å | ||||||
Authors | Smith, G.D. / Pangborn, W.A. / Blessing, R.H. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Phase changes in T(3)R(3)(f) human insulin: temperature or pressure induced? Authors: Smith, G.D. / Pangborn, W.A. / Blessing, R.H. #1: Journal: Biochemistry / Year: 1995 Title: X-ray Crystallographic Studies on Hexameric Insulins in the Presence of Helix-Stabilizing Agents, Thiocyanate, Methylparaben, and Phenol Authors: Whittingham, J.L. / Chaudhuri, S. / Dodson, E.J. / Moody, P.C.E. / Dodson, G.G. #2: Journal: Biochemistry / Year: 1994 Title: Crystallographic Evidence for Dual Coordination around Zinc in the T3R3 Human Insulin Hexamer Authors: Ciszak, E. / Smith, G.D. #3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1984 Title: Structural stability in the 4-zinc human insulin hexamer Authors: Smith, G.D. / Swenson, D.C. / Dodson, E.J. / Dodson, G.G. / Reynolds, C.D. #4: Journal: Nature / Year: 1976 Title: Structure of 4-zinc insulin Authors: Bentley, G. / Dodson, E. / Dodson, G.G. / Hodgkin, D. / Mercola, D. #5: Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: The First Protein Crystal Structure Determined from High Resolution X-Ray Powder Diffraction Data: A Variant of T3R3 Human Insulin Zinc Complex Produced by Grinding Authors: Von Dreele, R.B. / Stephens, P.W. / Smith, G.D. / Blessing, R.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g7a.cif.gz | 100.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g7a.ent.gz | 79.5 KB | Display | PDB format |
PDBx/mmJSON format | 1g7a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g7a_validation.pdf.gz | 493.1 KB | Display | wwPDB validaton report |
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Full document | 1g7a_full_validation.pdf.gz | 497.3 KB | Display | |
Data in XML | 1g7a_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | 1g7a_validation.cif.gz | 21.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g7/1g7a ftp://data.pdbj.org/pub/pdb/validation_reports/g7/1g7a | HTTPS FTP |
-Related structure data
Related structure data | 1g7bC 1trzS 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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2 |
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Unit cell |
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Components on special symmetry positions |
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Details | The second dimer of the T3R3 insulin hexamer is generated by the crystallographic three-fold axis: -y, x-y, z / The third dimer of the T3R3 insulin hexamer is generated by the crystallographic three-fold axis: y-x, -x, z |
-Components
-Protein/peptide , 2 types, 8 molecules ACEGBDFH
#1: Protein/peptide | Mass: 2383.698 Da / Num. of mol.: 4 / Fragment: A-CHAIN / Source method: obtained synthetically Details: This sequence occurs naturally in homo sapiens (Human) References: UniProt: P01308 #2: Protein/peptide | Mass: 3433.953 Da / Num. of mol.: 4 / Fragment: B-CHAIN / Source method: obtained synthetically Details: This sequence occurs naturally in homo sapiens (Human) References: UniProt: P01308 |
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-Non-polymers , 5 types, 292 molecules
#3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-CL / #5: Chemical | #6: Chemical | ChemComp-GOL / | #7: 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: 1.9 Å3/Da / Density % sol: 35.26 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: slow cooling / pH: 6.3 Details: 5 mg/ml human insulin, 0.01 M HCl, 0.007 M zinc acetate, 0.05 M sodium citrate, 17% acetone, 1.0 M NaCl. pH 6.3, SLOW COOLING at 298K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: microgravity | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X8C / Wavelength: 0.8 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 20, 1999 |
Radiation | Monochromator: Silicon / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→31.2 Å / Num. all: 53646 / Num. obs: 53646 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.6 % / Biso Wilson estimate: 17.6 Å2 / Rmerge(I) obs: 0.049 / Net I/σ(I): 42.8 |
Reflection shell | Resolution: 1.2→1.23 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.299 / Mean I/σ(I) obs: 7.1 / Num. unique all: 3598 / % possible all: 100 |
Reflection | *PLUS % possible obs: 100 % / Num. measured all: 925256 |
Reflection shell | *PLUS % possible obs: 75.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB Entry 1trz Resolution: 1.2→31.2 Å / Rfactor Rfree error: 0.003 / Isotropic thermal model: Restrained / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 73.9 Å2 / ksol: 0.44 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.2→31.2 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.2→1.28 Å / Rfactor Rfree error: 0.009 / Total num. of bins used: 6
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.2 Å / Lowest resolution: 31.2 Å / σ(F): 0 / % reflection Rfree: 10.2 % / Rfactor obs: 0.169 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.259 / % reflection Rfree: 9.9 % / Rfactor Rwork: 0.24 |