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- PDB-5boq: Human insulin with intra-chain chemical crosslink between modifie... -

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Basic information

Entry
Database: PDB / ID: 5boq
TitleHuman insulin with intra-chain chemical crosslink between modified B24 and B29
Components(Insulin) x 2
KeywordsHORMONE / Chemical crosslink / B24-B29 / specificity
Function / homology
Function and homology information


Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / Insulin processing / IRS activation / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of feeding behavior / negative regulation of fatty acid metabolic process ...Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / Insulin processing / IRS activation / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of feeding behavior / negative regulation of fatty acid metabolic process / regulation of protein secretion / Regulation of gene expression in beta cells / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / negative regulation of respiratory burst involved in inflammatory response / negative regulation of gluconeogenesis / negative regulation of reactive oxygen species biosynthetic process / positive regulation of cellular protein metabolic process / regulation of protein localization to plasma membrane / COPI-mediated anterograde transport / Regulation of insulin secretion / positive regulation of dendritic spine maintenance / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of glycogen biosynthetic process / regulation of cellular amino acid metabolic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of nitric oxide mediated signal transduction / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / Signal attenuation / negative regulation of lipid catabolic process / negative regulation of protein secretion / positive regulation of lipid biosynthetic process / fatty acid homeostasis / endosome lumen / transport vesicle / positive regulation of insulin receptor signaling pathway / endoplasmic reticulum-Golgi intermediate compartment membrane / neuron projection maintenance / insulin-like growth factor receptor binding / positive regulation of protein autophosphorylation / positive regulation of glycolytic process / negative regulation of acute inflammatory response / regulation of transmembrane transporter activity / positive regulation of cell differentiation / Insulin receptor signalling cascade / positive regulation of mitotic nuclear division / regulation of synaptic plasticity / positive regulation of brown fat cell differentiation / cognition / regulation of protein localization / positive regulation of long-term synaptic potentiation / positive regulation of cytokine production / acute-phase response / activation of protein kinase B activity / positive regulation of glucose import / vasodilation / 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 / glucose metabolic process / Golgi lumen / positive regulation of nitric-oxide synthase activity / cell-cell signaling / glucose homeostasis / wound healing / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of MAPK cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of phosphatidylinositol 3-kinase signaling / positive regulation of cell growth / secretory granule lumen / protease binding / positive regulation of NF-kappaB transcription factor activity / positive regulation of cell migration / positive regulation of protein kinase B signaling / Amyloid fiber formation / Golgi membrane / G protein-coupled receptor signaling pathway / amyloid fibril formation / endoplasmic reticulum lumen / regulation of transcription, DNA-templated / positive regulation of gene expression / positive regulation of cell population proliferation / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin-like superfamily / Insulin family signature.
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsBrzozowski, A.M. / Turkenburg, J.P. / Jiracek, J. / Zakova, L.
Funding support United Kingdom, Czech Republic, 2items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)MR/K000179/1 United Kingdom
Czech Academy of SciencesRVO:61388963 Czech Republic
CitationJournal: Sci Rep / Year: 2016
Title: Rational steering of insulin binding specificity by intra-chain chemical crosslinking.
Authors: Vikova, J. / Collinsova, M. / Kletvikova, E. / Budesinsky, M. / Kaplan, V. / Zakova, L. / Veverka, V. / Hexnerova, R. / Avino, R.J. / Strakova, J. / Selicharova, I. / Vanek, V. / Wright, D.W. ...Authors: Vikova, J. / Collinsova, M. / Kletvikova, E. / Budesinsky, M. / Kaplan, V. / Zakova, L. / Veverka, V. / Hexnerova, R. / Avino, R.J. / Strakova, J. / Selicharova, I. / Vanek, V. / Wright, D.W. / Watson, C.J. / Turkenburg, J.P. / Brzozowski, A.M. / Jiracek, J.
History
DepositionMay 27, 2015Deposition site: RCSB / Processing site: PDBE
Revision 1.0Feb 3, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Insulin
B: Insulin
C: Insulin
D: Insulin
E: Insulin
F: Insulin
G: Insulin
H: Insulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,45911
Polymers23,1708
Non-polymers2883
Water3,603200
1
A: Insulin
B: Insulin
E: Insulin
F: Insulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,6815
Polymers11,5854
Non-polymers961
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3940 Å2
ΔGint-46 kcal/mol
Surface area5980 Å2
MethodPISA
2
C: Insulin
D: Insulin
G: Insulin
H: Insulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,7776
Polymers11,5854
Non-polymers1922
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3550 Å2
ΔGint-60 kcal/mol
Surface area4800 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)55.438, 56.865, 60.012
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein/peptide
Insulin /


Mass: 2383.698 Da / Num. of mol.: 4 / Fragment: UNP residues 90-110 / Source method: obtained synthetically / Details: Sequence occurs naturally / Source: (synth.) Homo sapiens (human) / References: UniProt: P01308
#2: Protein/peptide
Insulin /


Mass: 3408.885 Da / Num. of mol.: 4 / Fragment: UNP residues 25-54 / Source method: obtained synthetically / Details: covalent cross-link between modified B24 and B29 / Source: (synth.) Homo sapiens (human) / References: UniProt: P01308
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 200 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.37 Å3/Da / Density % sol: 48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 3 / Details: 0.1 M (NH4)2SO4, 1% (v/v) dioxane

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 22, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 1.7→41.28 Å / Num. all: 19860 / Num. obs: 19860 / % possible obs: 92.6 % / Redundancy: 6.2 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 15.7
Reflection shellResolution: 1.7→1.73 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 4.3 / % possible all: 60.5

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Processing

Software
NameVersionClassification
REFMAC5.8.0124refinement
xia2data scaling
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1mso
Resolution: 1.7→60.01 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.936 / SU B: 2.338 / SU ML: 0.077 / Cross valid method: THROUGHOUT / ESU R: 0.125 / ESU R Free: 0.12 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23215 922 4.7 %RANDOM
Rwork0.19571 ---
obs0.19747 18898 92.16 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.567 Å2
Baniso -1Baniso -2Baniso -3
1-0.12 Å2-0 Å2-0 Å2
2---0.34 Å20 Å2
3---0.22 Å2
Refinement stepCycle: LAST / Resolution: 1.7→60.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1385 0 15 200 1600
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.0191438
X-RAY DIFFRACTIONr_bond_other_d0.0020.021270
X-RAY DIFFRACTIONr_angle_refined_deg2.3631.9951959
X-RAY DIFFRACTIONr_angle_other_deg1.10132920
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.6055177
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.29825.57461
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.92815214
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.702152
X-RAY DIFFRACTIONr_chiral_restr0.1170.2223
X-RAY DIFFRACTIONr_gen_planes_refined0.010.021634
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02324
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.9651.768726
X-RAY DIFFRACTIONr_mcbond_other1.8711.762725
X-RAY DIFFRACTIONr_mcangle_it2.8252.624894
X-RAY DIFFRACTIONr_mcangle_other2.832.63895
X-RAY DIFFRACTIONr_scbond_it2.7352.092712
X-RAY DIFFRACTIONr_scbond_other2.6032.065701
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.0483.0171049
X-RAY DIFFRACTIONr_long_range_B_refined6.31816.2191697
X-RAY DIFFRACTIONr_long_range_B_other6.07115.6321614
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.7→1.744 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.263 40 -
Rwork0.205 908 -
obs--60.85 %

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