[English] 日本語
Yorodumi
- PDB-4evp: Crystal Structure of Mouse Catenin beta-59 in 7.2M urea -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4evp
TitleCrystal Structure of Mouse Catenin beta-59 in 7.2M urea
ComponentsCatenin beta-1
KeywordsCELL ADHESION / mouse beta catenin / urea
Function / homology
Function and homology information


lung cell differentiation / epicardium-derived cardiac vascular smooth muscle cell differentiation / mesenchyme morphogenesis / RUNX3 regulates WNT signaling / Regulation of CDH11 function / cardiac vascular smooth muscle cell differentiation / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / Beta-catenin phosphorylation cascade / Apoptotic cleavage of cell adhesion proteins / Disassembly of the destruction complex and recruitment of AXIN to the membrane ...lung cell differentiation / epicardium-derived cardiac vascular smooth muscle cell differentiation / mesenchyme morphogenesis / RUNX3 regulates WNT signaling / Regulation of CDH11 function / cardiac vascular smooth muscle cell differentiation / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / Beta-catenin phosphorylation cascade / Apoptotic cleavage of cell adhesion proteins / Disassembly of the destruction complex and recruitment of AXIN to the membrane / hair cycle process / morphogenesis of embryonic epithelium / positive regulation of epithelial cell differentiation / TCF dependent signaling in response to WNT / LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production / trachea morphogenesis / mesenchyme development / endoderm formation / Formation of the beta-catenin:TCF transactivating complex / VEGFR2 mediated vascular permeability / Deactivation of the beta-catenin transactivating complex / positive regulation of heparan sulfate proteoglycan biosynthetic process / lung induction / positive regulation of branching involved in lung morphogenesis / cranial ganglion development / renal vesicle formation / renal inner medulla development / renal outer medulla development / nephron tubule formation / mesenchymal stem cell differentiation / beta-catenin-ICAT complex / metanephros morphogenesis / genitalia morphogenesis / embryonic skeletal limb joint morphogenesis / neural plate development / glial cell fate determination / regulation of secondary heart field cardioblast proliferation / astrocyte-dopaminergic neuron signaling / canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation / oviduct development / beta-catenin-TCF7L2 complex / regulation of nephron tubule epithelial cell differentiation / negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis / regulation of timing of anagen / negative regulation of mitotic cell cycle, embryonic / regulation of epithelial cell differentiation / Ca2+ pathway / Schwann cell proliferation / central nervous system vasculogenesis / animal organ development / regulation of centriole-centriole cohesion / Adherens junctions interactions / RHO GTPases activate IQGAPs / glandular epithelial cell differentiation / regulation of centromeric sister chromatid cohesion / Degradation of beta-catenin by the destruction complex / ventricular compact myocardium morphogenesis / embryonic axis specification / endodermal cell fate commitment / Scrib-APC-beta-catenin complex / lens morphogenesis in camera-type eye / positive regulation of fibroblast growth factor receptor signaling pathway / mesenchymal cell proliferation involved in lung development / beta-catenin-TCF complex / dorsal root ganglion development / synaptic vesicle clustering / acinar cell differentiation / proximal/distal pattern formation / neuron fate determination / layer formation in cerebral cortex / dorsal/ventral axis specification / positive regulation of endothelial cell differentiation / positive regulation of myoblast proliferation / establishment of blood-retinal barrier / fungiform papilla formation / sympathetic ganglion development / delta-catenin binding / embryonic foregut morphogenesis / hindbrain development / lung epithelial cell differentiation / positive regulation of determination of dorsal identity / ectoderm development / positive regulation of skeletal muscle tissue development / regulation of calcium ion import / regulation of protein localization to cell surface / regulation of osteoclast differentiation / cellular response to indole-3-methanol / endothelial tube morphogenesis / cell projection membrane / smooth muscle cell differentiation / presynaptic active zone cytoplasmic component / positive regulation of odontoblast differentiation / regulation of smooth muscle cell proliferation / cranial skeletal system development / midbrain dopaminergic neuron differentiation / histone methyltransferase binding / mesenchymal cell proliferation / alpha-catenin binding / lung-associated mesenchyme development / establishment of blood-brain barrier
Similarity search - Function
Beta-catenin / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / Leucine-rich Repeat Variant / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
UREA / Catenin beta-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.255 Å
AuthorsWang, C. / Zhang, G.Y.
CitationJournal: TO BE PUBLISHED
Title: Crystal Structure of Mouse Catenin beta-59 in 7.2M urea
Authors: Wang, C. / Zhang, G.Y.
History
DepositionApr 26, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 1, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Catenin beta-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,42644
Polymers58,8441
Non-polymers2,58243
Water3,441191
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)64.154, 102.441, 186.871
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-701-

URE

21A-701-

URE

31A-801-

HOH

41A-810-

HOH

-
Components

#1: Protein Catenin beta-1 / Beta-catenin


Mass: 58844.117 Da / Num. of mol.: 1 / Fragment: unp residues 134-671
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ctnnb1, Catnb / Production host: Escherichia coli (E. coli) / References: UniProt: Q02248
#2: Chemical...
ChemComp-URE / UREA


Mass: 60.055 Da / Num. of mol.: 43 / Source method: obtained synthetically / Formula: CH4N2O
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 191 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.61 Å3/Da / Density % sol: 52.85 %
Crystal growMethod: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 10, 2010
RadiationMonochromator: 0.99 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.255→46.995 Å / Num. obs: 29497 / % possible obs: 99.34 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 14.5 % / Rmerge(I) obs: 0.109 / Net I/σ(I): 22.06
Reflection shellResolution: 2.25→2.3 Å / Redundancy: 14.1 % / Rmerge(I) obs: 0.729 / Mean I/σ(I) obs: 3.78 / % possible all: 100

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
AMoREphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.255→46.995 Å / SU ML: 0.21 / σ(F): 1.34 / Phase error: 22.24 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2253 1494 5.08 %
Rwork0.1907 --
obs0.1925 29433 99.77 %
all-33637 -
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 41.028 Å2 / ksol: 0.331 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.7073 Å20 Å2-0 Å2
2--9.1441 Å20 Å2
3----8.4369 Å2
Refinement stepCycle: LAST / Resolution: 2.255→46.995 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3725 0 172 191 4088
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0053919
X-RAY DIFFRACTIONf_angle_d0.9585273
X-RAY DIFFRACTIONf_dihedral_angle_d13.5281413
X-RAY DIFFRACTIONf_chiral_restr0.061627
X-RAY DIFFRACTIONf_plane_restr0.004702
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2548-2.32760.28561480.22932462X-RAY DIFFRACTION98
2.3276-2.41080.2811370.2132506X-RAY DIFFRACTION100
2.4108-2.50730.27271310.20592490X-RAY DIFFRACTION100
2.5073-2.62140.22711330.19892527X-RAY DIFFRACTION100
2.6214-2.75960.24731310.20152528X-RAY DIFFRACTION100
2.7596-2.93250.23221180.20072536X-RAY DIFFRACTION100
2.9325-3.15880.2211270.20182533X-RAY DIFFRACTION100
3.1588-3.47660.24051320.20032540X-RAY DIFFRACTION100
3.4766-3.97950.20511310.17282573X-RAY DIFFRACTION100
3.9795-5.01280.20621510.16512576X-RAY DIFFRACTION100
5.0128-47.00560.2151550.19822668X-RAY DIFFRACTION100

+
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