[English] 日本語
Yorodumi
- PDB-1pid: BOVINE DESPENTAPEPTIDE INSULIN -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1pid
TitleBOVINE DESPENTAPEPTIDE INSULIN
Components(DESPENTAPEPTIDE INSULIN) x 2
KeywordsHORMONE / GLUCOSE METABOLISM
Function / homology
Function and homology information


estradiol secretion / negative regulation of lactation / positive regulation of blood circulation / glucose import in response to insulin stimulus / positive regulation of cell maturation / positive regulation of lactation / response to L-arginine / positive regulation of mammary gland epithelial cell proliferation / negative regulation of appetite / response to butyrate ...estradiol secretion / negative regulation of lactation / positive regulation of blood circulation / glucose import in response to insulin stimulus / positive regulation of cell maturation / positive regulation of lactation / response to L-arginine / positive regulation of mammary gland epithelial cell proliferation / negative regulation of appetite / response to butyrate / feeding behavior / response to growth hormone / response to food / positive regulation of Rho protein signal transduction / positive regulation of peptide hormone secretion / protein secretion / response to glucose / negative regulation of lipid catabolic process / response to nutrient levels / positive regulation of protein secretion / insulin receptor binding / hormone activity / positive regulation of insulin secretion / glucose metabolic process / glucose homeostasis / response to heat / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of gene expression / negative regulation of apoptotic process / extracellular space / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily
Similarity search - Domain/homology
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / Resolution: 1.3 Å
AuthorsHolden, P.H. / Papiz, M. / Dodson, G.G.
Citation
Journal: Proteins / Year: 1997
Title: A model of insulin fibrils derived from the x-ray crystal structure of a monomeric insulin (despentapeptide insulin).
Authors: Brange, J. / Dodson, G.G. / Edwards, D.J. / Holden, P.H. / Whittingham, J.L.
#1: Journal: Acta Crystallogr.,Sect.B / Year: 1983
Title: Molecular Replacement Studies on Crystal Forms of Despentapeptide Insulin
Authors: Bi, R.-C. / Cutfield, S.M. / Dodson, E.J. / Dodson, G.G. / Giordano, F. / Reynolds, C.D. / Tolley, S.P.
History
DepositionNov 22, 1995-
Revision 1.0Dec 7, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 16, 2011Group: Atomic model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DESPENTAPEPTIDE INSULIN
B: DESPENTAPEPTIDE INSULIN
C: DESPENTAPEPTIDE INSULIN
D: DESPENTAPEPTIDE INSULIN


Theoretical massNumber of molelcules
Total (without water)10,3644
Polymers10,3644
Non-polymers00
Water1,62190
1
A: DESPENTAPEPTIDE INSULIN
B: DESPENTAPEPTIDE INSULIN


Theoretical massNumber of molelcules
Total (without water)5,1822
Polymers5,1822
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: DESPENTAPEPTIDE INSULIN
D: DESPENTAPEPTIDE INSULIN


Theoretical massNumber of molelcules
Total (without water)5,1822
Polymers5,1822
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)52.700, 26.180, 51.710
Angle α, β, γ (deg.)90.00, 93.00, 90.00
Int Tables number5
Space group name H-MC1211
Components on special symmetry positions
IDModelComponents
11B-98-

HOH

Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.99439, 0.035258, 0.099728), (-0.045704, 0.993476, 0.10448), (-0.095394, -0.108451, 0.989514)
Vector: -5.47395, -1.22199, 27.14091)

-
Components

#1: Protein/peptide DESPENTAPEPTIDE INSULIN


Mass: 2339.645 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P01317
#2: Protein/peptide DESPENTAPEPTIDE INSULIN


Mass: 2842.277 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P01317
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 90 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION

-
Sample preparation

CrystalDensity Matthews: 1.72 Å3/Da / Density % sol: 28.43 %
Crystal grow
*PLUS
Method: batch method
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
20.02 MTris-HCl115.0ml
30.05 Mtrisodium citrate115.0ml
440 %satammonium sulfate111.5ml
60.1 Mcitric acid11
1depentapeptide insulin1115 mg
5acetone111.5ml

-
Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Num. obs: 31367 / % possible obs: 90.7 %

-
Processing

SoftwareName: PROLSQ / Classification: refinement
RefinementResolution: 1.3→25.4 Å / σ(F): 0 /
Num. reflection% reflection
obs16916 90.7 %
Refinement stepCycle: LAST / Resolution: 1.3→25.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms730 0 0 90 820
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.010.02
X-RAY DIFFRACTIONp_angle_d0.030.04
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.030.06
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it2.2593
X-RAY DIFFRACTIONp_mcangle_it2.443.5
X-RAY DIFFRACTIONp_scbond_it4.5273
X-RAY DIFFRACTIONp_scangle_it4.4753.5
X-RAY DIFFRACTIONp_plane_restr0.010.02
X-RAY DIFFRACTIONp_chiral_restr0.080.1
X-RAY DIFFRACTIONp_singtor_nbd0.160.5
X-RAY DIFFRACTIONp_multtor_nbd0.270.5
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd0.310.5
X-RAY DIFFRACTIONp_planar_tor2.420
X-RAY DIFFRACTIONp_staggered_tor14.420
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor16.320
X-RAY DIFFRACTIONp_special_tor
Refinement
*PLUS
Rfactor obs: 0.19
Solvent computation
*PLUS
Displacement parameters
*PLUS

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more