+Open data
-Basic information
Entry | Database: PDB / ID: 1dei | ||||||
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Title | DESHEPTAPEPTIDE (B24-B30) INSULIN | ||||||
Components | (INSULIN) x 2 | ||||||
Keywords | HORMONE / GLUCOSE METABOLISM | ||||||
Function / homology | Function and homology information Insulin processing / IRS activation / Signal attenuation / Insulin receptor signalling cascade / Signaling by Insulin receptor / Synthesis, secretion, and deacylation of Ghrelin / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Insulin receptor recycling / glycoprotein biosynthetic process / response to L-arginine ...Insulin processing / IRS activation / Signal attenuation / Insulin receptor signalling cascade / Signaling by Insulin receptor / Synthesis, secretion, and deacylation of Ghrelin / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Insulin receptor recycling / glycoprotein biosynthetic process / response to L-arginine / positive regulation of lipoprotein lipase activity / lactate biosynthetic process / positive regulation of fatty acid biosynthetic process / positive regulation of glucose metabolic process / lipoprotein biosynthetic process / COPI-mediated anterograde transport / lipid biosynthetic process / positive regulation of DNA replication / negative regulation of gluconeogenesis / positive regulation of insulin receptor signaling pathway / positive regulation of protein autophosphorylation / insulin-like growth factor receptor binding / positive regulation of protein secretion / hormone activity / glucose metabolic process / glucose homeostasis / insulin receptor signaling pathway / positive regulation of cell migration / extracellular space / identical protein binding Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Bao, S.-J. / Chang, W.-R. / Wan, Z.-L. / Zhang, J.-P. / Liang, D.-C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Crystal structure of desheptapeptide(B24-B30)insulin at 1.6 A resolution: implications for receptor binding. Authors: Bao, S.J. / Xie, D.L. / Zhang, J.P. / Chang, W.R. / Liang, D.C. #1: Journal: Sci.Sin., Ser.B (Engl.Ed.) / Year: 1987 Title: Refinement of the Structure of Despentapeptide (B26-B30) Insulin at 1.5 Angstroms Resolution Authors: Dai, J.B. / Lou, M.Z. / You, J.M. / Liang, D.C. #2: Journal: Sci.Sin., Ser.B (Engl.Ed.) / Year: 1982 Title: Crystallographic Studies on Desheptapeptide(B24-B30) Insulin-Growth of Single Crystals and Determination of its Crystallographic Parameters Authors: Chang, W.R. / Xie, D.L. / Liang, D.C. / al., et | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dei.cif.gz | 28.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dei.ent.gz | 19.8 KB | Display | PDB format |
PDBx/mmJSON format | 1dei.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dei_validation.pdf.gz | 436.1 KB | Display | wwPDB validaton report |
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Full document | 1dei_full_validation.pdf.gz | 437 KB | Display | |
Data in XML | 1dei_validation.xml.gz | 6.7 KB | Display | |
Data in CIF | 1dei_validation.cif.gz | 8.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/de/1dei ftp://data.pdbj.org/pub/pdb/validation_reports/de/1dei | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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Details | THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT OF INSULIN CONSISTS OF TWO INSULIN MOLECULES EACH CONSISTING OF TWO CHAINS. THIS ENTRY PRESENTS COORDINATES FOR MOLECULES I (CHAIN IDENTIFIERS *A* AND *B*) AND II (CHAIN IDENTIFIERS *C* AND *D*). |
-Components
#1: Protein/peptide | Mass: 2383.698 Da / Num. of mol.: 2 / Mutation: CHAIN B, DEL(24-30) Source method: isolated from a genetically manipulated source Details: DESHEPTAPEPTIDE (B24-B30) / Source: (gene. exp.) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P01315 #2: Protein/peptide | Mass: 2547.929 Da / Num. of mol.: 2 / Mutation: CHAIN B, DEL(24-30) Source method: isolated from a genetically manipulated source Details: DESHEPTAPEPTIDE (B24-B30) / Source: (gene. exp.) Sus scrofa (pig) / Organ: PANCREAS / References: UniProt: P01315 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 1.88 Å3/Da / Density % sol: 35 % |
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Crystal grow | *PLUS Method: other / Details: Chang, W.R., (1982) Sci. Sin. Ser. B, 25, 385. |
-Data collection
Diffraction | Mean temperature: 293.1 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: STOE / Detector: DIFFRACTOMETER / Date: May 11, 1985 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→8 Å / Num. obs: 8331 / % possible obs: 81.1 % / Observed criterion σ(I): 1 / Redundancy: 2 % / Rmerge(I) obs: 0.088 |
Reflection shell | Resolution: 1.6→1.63 Å / % possible all: 44.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: DESPENTAPEPTIDE(B26-B30)INSULIN Resolution: 1.6→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 14.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.63 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rwork: 0.26 |