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- PDB-1h6g: alpha-catenin M-domain -

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Basic information

Entry
Database: PDB / ID: 1h6g
Titlealpha-catenin M-domain
ComponentsALPHA-1 CATENIN
KeywordsCELL ADHESION / ALPHA-CATENIN / ADHESION MODULATION / CYTOSKELETON
Function / homology
Function and homology information


negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gamma-catenin binding / epithelial cell-cell adhesion / zonula adherens / gap junction assembly / cellular response to indole-3-methanol / vinculin binding ...negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gamma-catenin binding / epithelial cell-cell adhesion / zonula adherens / gap junction assembly / cellular response to indole-3-methanol / vinculin binding / negative regulation of cell motility / flotillin complex / apical junction assembly / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of smoothened signaling pathway / catenin complex / Adherens junctions interactions / negative regulation of protein localization to nucleus / axon regeneration / negative regulation of neuroblast proliferation / smoothened signaling pathway / establishment or maintenance of cell polarity / Myogenesis / odontogenesis of dentin-containing tooth / intercalated disc / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / neuroblast proliferation / RHO GTPases activate IQGAPs / extrinsic apoptotic signaling pathway in absence of ligand / ovarian follicle development / acrosomal vesicle / VEGFR2 mediated vascular permeability / integrin-mediated signaling pathway / adherens junction / beta-catenin binding / cell-cell adhesion / response to estrogen / male gonad development / actin filament binding / cell-cell junction / protein localization / cell migration / actin cytoskeleton / cell junction / lamellipodium / cell adhesion / cadherin binding / intracellular membrane-bounded organelle / focal adhesion / structural molecule activity / RNA binding / identical protein binding / nucleus / plasma membrane / cytosol
Similarity search - Function
Alpha-catenin / Alpha-catenin/vinculin-like / Vinculin, conserved site / Vinculin family talin-binding region signature. / Vinculin/alpha-catenin / Vinculin family / Alpha-catenin/vinculin-like superfamily / Four Helix Bundle (Hemerythrin (Met), subunit A) / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.2 Å
AuthorsYang, J. / Dokurno, P. / Tonks, N.K. / Barford, D.
CitationJournal: Embo J. / Year: 2001
Title: Crystal Structure of the M-Fragment of Alpha-Catenin: Implications for Modulation of Cell Adhesion.
Authors: Yang, J. / Dokurno, P. / Tonks, N.K. / Barford, D.
History
DepositionJun 14, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 7, 2001Provider: repository / Type: Initial release
Revision 1.1Feb 10, 2016Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Other / Refinement description / Structure summary / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ALPHA-1 CATENIN
B: ALPHA-1 CATENIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,9956
Polymers57,7612
Non-polymers2344
Water7,080393
1
A: ALPHA-1 CATENIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,0744
Polymers28,8811
Non-polymers1943
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: ALPHA-1 CATENIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)28,9212
Polymers28,8811
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)42.863, 85.703, 75.481
Angle α, β, γ (deg.)90.00, 100.47, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein ALPHA-1 CATENIN / CADHERIN-ASSOCIATED PROTEIN / ALPHA E-CATENIN


Mass: 28880.719 Da / Num. of mol.: 2 / Fragment: M-FRAGMENT, RESIDUES 377-632
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET28M / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): B834 / References: UniProt: P35221
#2: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 393 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.43 Å3/Da / Density % sol: 49 %
Crystal growpH: 4.6
Details: 30 % (V/V) MPD, 0.1 M SODIUM ACETETE BUFFER, PH 4.6, 20 MM CALCIUM CHLORIDE
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / Details: used microseeding
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
130 %MPD1reservoir
20.1 Msodium acetate1reservoir
320 mM1reservoirCaCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SRS / Beamline: PX14.1 / Wavelength: 1.488
DetectorType: ADSC IMAGE PLATE / Detector: IMAGE PLATE / Date: Sep 8, 2000
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.488 Å / Relative weight: 1
ReflectionResolution: 2.2→30 Å / Num. obs: 27803 / % possible obs: 99.1 % / Redundancy: 6.2 % / Biso Wilson estimate: 28.6 Å2 / Rmerge(I) obs: 0.049 / Net I/σ(I): 13.3
Reflection shellResolution: 2.2→2.25 Å / Rmerge(I) obs: 0.205 / % possible all: 98.4
Reflection
*PLUS
Num. measured all: 171946
Reflection shell
*PLUS
% possible obs: 98.4 %

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
SHARPphasing
CNS1refinement
RefinementMethod to determine structure: MAD / Resolution: 2.2→24.74 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 11930144.31 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflectionSelection details
Rfree0.257 1370 5.1 %RANDOM
Rwork0.193 ---
obs0.193 27080 99.1 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 87.3308 Å2 / ksol: 0.330463 e/Å3
Displacement parametersBiso mean: 44.6 Å2
Baniso -1Baniso -2Baniso -3
1--6.42 Å20 Å2-1.23 Å2
2--0.82 Å20 Å2
3---5.6 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.32 Å0.23 Å
Luzzati d res low-5 Å
Luzzati sigma a0.22 Å0.17 Å
Refinement stepCycle: LAST / Resolution: 2.2→24.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3792 0 11 393 4196
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.014
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.5
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d18
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d1.12
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.591.5
X-RAY DIFFRACTIONc_mcangle_it2.532
X-RAY DIFFRACTIONc_scbond_it2.682
X-RAY DIFFRACTIONc_scangle_it3.922.5
LS refinement shellResolution: 2.2→2.34 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.29 242 5.4 %
Rwork0.21 4244 -
obs--98.9 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION3ION.PARAMION.TOP
X-RAY DIFFRACTION4MPD.PARAMMPD.TOPOLOGY
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.0145
X-RAY DIFFRACTIONc_angle_deg1.51
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg18
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.12
LS refinement shell
*PLUS
Rfactor Rfree: 0.29 / Rfactor Rwork: 0.21

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