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Yorodumi- PDB-1ir3: PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH P... -
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-Basic information
Entry | Database: PDB / ID: 1ir3 | ||||||
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Title | PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG | ||||||
Components |
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Keywords | COMPLEX (TRANSFERASE/SUBSTRATE) / TYROSINE KINASE / SIGNAL TRANSDUCTION / PHOSPHOTRANSFERASE / COMPLEX (KINASE-PEPTIDE SUBSTRATE-ATP ANALOG) / ENZYME / COMPLEX (TRANSFERASE-SUBSTRATE) / COMPLEX (TRANSFERASE-SUBSTRATE) complex | ||||||
Function / homology | Function and homology information regulation of female gonad development / positive regulation of meiotic cell cycle / insulin-like growth factor II binding / positive regulation of developmental growth / male sex determination / exocrine pancreas development / insulin receptor complex / insulin-like growth factor I binding / insulin receptor activity / positive regulation of protein-containing complex disassembly ...regulation of female gonad development / positive regulation of meiotic cell cycle / insulin-like growth factor II binding / positive regulation of developmental growth / male sex determination / exocrine pancreas development / insulin receptor complex / insulin-like growth factor I binding / insulin receptor activity / positive regulation of protein-containing complex disassembly / cargo receptor activity / dendritic spine maintenance / insulin binding / PTB domain binding / adrenal gland development / Signaling by Insulin receptor / IRS activation / activation of protein kinase activity / neuronal cell body membrane / amyloid-beta clearance / positive regulation of respiratory burst / positive regulation of receptor internalization / regulation of embryonic development / insulin receptor substrate binding / transport across blood-brain barrier / positive regulation of glycogen biosynthetic process / epidermis development / Signal attenuation / phosphatidylinositol 3-kinase binding / heart morphogenesis / Insulin receptor recycling / insulin-like growth factor receptor binding / dendrite membrane / neuron projection maintenance / activation of protein kinase B activity / positive regulation of glycolytic process / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / receptor-mediated endocytosis / positive regulation of MAP kinase activity / learning / caveola / positive regulation of glucose import / receptor protein-tyrosine kinase / peptidyl-tyrosine phosphorylation / cellular response to insulin stimulus / receptor internalization / memory / cellular response to growth factor stimulus / male gonad development / positive regulation of nitric oxide biosynthetic process / glucose homeostasis / late endosome / insulin receptor signaling pathway / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / amyloid-beta binding / protein tyrosine kinase activity / protein autophosphorylation / receptor complex / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endosome membrane / lysosome / positive regulation of cell migration / positive regulation of protein phosphorylation / symbiont entry into host cell / protein domain specific binding / G protein-coupled receptor signaling pathway / protein phosphorylation / external side of plasma membrane / axon / positive regulation of cell population proliferation / positive regulation of DNA-templated transcription / regulation of DNA-templated transcription / protein-containing complex binding / GTP binding / extracellular exosome / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Hubbard, S.R. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. Authors: Hubbard, S.R. #1: Journal: Nature / Year: 1994 Title: Crystal Structure of the Tyrosine Kinase Domain of the Human Insulin Receptor Authors: Hubbard, S.R. / Wei, L. / Ellis, L. / Hendrickson, W.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ir3.cif.gz | 78 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ir3.ent.gz | 59.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ir3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ir3_validation.pdf.gz | 746.7 KB | Display | wwPDB validaton report |
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Full document | 1ir3_full_validation.pdf.gz | 747.9 KB | Display | |
Data in XML | 1ir3_validation.xml.gz | 15.8 KB | Display | |
Data in CIF | 1ir3_validation.cif.gz | 22.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ir/1ir3 ftp://data.pdbj.org/pub/pdb/validation_reports/ir/1ir3 | HTTPS FTP |
-Related structure data
Related structure data | 1irkS 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: 35032.738 Da / Num. of mol.: 1 / Fragment: TYROSINE KINASE DOMAIN / Mutation: C981S, Y984F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location (production host): CYTOPLASM / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 / References: UniProt: P06213, EC: 2.7.1.112 | ||||
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#2: Protein/peptide | Mass: 1955.280 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source | ||||
#3: Chemical | #4: Chemical | ChemComp-ANP / | #5: 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: 2.4 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: 22% PEG 8000, 100 MM TRIS-HCL, PH 7.5, 2% ETHYLENE GLYCOL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.9796 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Jun 1, 1996 / Details: MIRROR |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9796 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 28286 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Rmerge(I) obs: 0.065 / Rsym value: 0.065 / Net I/σ(I): 12.9 |
Reflection | *PLUS Num. measured all: 93535 |
Reflection shell | *PLUS % possible obs: 90.6 % / Rmerge(I) obs: 0.153 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1IRK Resolution: 1.9→6 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 18.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.97 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.816 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.189 |