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- PDB-1cws: HUMAN CDC25B CATALYTIC DOMAIN WITH TUNGSTATE -

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Basic information

Entry
Database: PDB / ID: 1cws
TitleHUMAN CDC25B CATALYTIC DOMAIN WITH TUNGSTATE
ComponentsCDC25 B-TYPE TYROSINE PHOSPHATASE
KeywordsCELL CYCLE / HYDROLASE / CELL CYCLE PHOSPHATASE / DUAL SPECIFICITY PROTEIN PHOSPHATASE / CDC25 / CDC25B
Function / homology
Function and homology information


positive regulation of G2/MI transition of meiotic cell cycle / female meiosis I / oocyte maturation / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / positive regulation of cytokinesis / phosphoprotein phosphatase activity / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / positive regulation of G2/M transition of mitotic cell cycle / positive regulation of mitotic cell cycle ...positive regulation of G2/MI transition of meiotic cell cycle / female meiosis I / oocyte maturation / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / positive regulation of cytokinesis / phosphoprotein phosphatase activity / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / positive regulation of G2/M transition of mitotic cell cycle / positive regulation of mitotic cell cycle / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / spindle pole / G2/M transition of mitotic cell cycle / mitotic cell cycle / cell division / protein phosphorylation / centrosome / positive regulation of cell population proliferation / protein kinase binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
M-phase inducer phosphatase / M-phase inducer phosphatase / Rhodanese-like domain / Oxidized Rhodanese; domain 1 / Rhodanese Homology Domain / Rhodanese-like domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / Rhodanese-like domain / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
BETA-MERCAPTOETHANOL / TUNGSTATE(VI)ION / M-phase inducer phosphatase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MIR / Resolution: 2 Å
AuthorsWatenpaugh, K.D. / Reynolds, R.A. / Chidester, C.G.
CitationJournal: J.Mol.Biol. / Year: 1999
Title: Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle.
Authors: Reynolds, R.A. / Yem, A.W. / Wolfe, C.L. / Deibel Jr., M.R. / Chidester, C.G. / Watenpaugh, K.D.
History
DepositionAug 26, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 30, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CDC25 B-TYPE TYROSINE PHOSPHATASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,3655
Polymers24,9071
Non-polymers4574
Water2,936163
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)51.734, 71.863, 74.935
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 1 molecules A

#1: Protein CDC25 B-TYPE TYROSINE PHOSPHATASE / M-PHASE INDUCER PHOSPHATASE 2 (CDC25B)


Mass: 24907.461 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOPLASM / Gene: CDC25B / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P30305

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Non-polymers , 5 types, 167 molecules

#2: Chemical ChemComp-WO4 / TUNGSTATE(VI)ION


Mass: 247.838 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: WO4
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-BME / BETA-MERCAPTOETHANOL


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 163 / 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: 2.79 Å3/Da / Density % sol: 55.99 %
Crystal growpH: 9
Details: 4 MICROLITERS PROTEIN (10 MG/ ML IN 50 MM TRISHCL, WO4=,1% BME AT PH 9.0) MIXED WITH 4 MICROLITERS WELL BUFFER (1.8 (NH4)2SO4, 0.5 M NACL, 0.1 M TRISHCL, 0.25 BME) AT 4 DEG. C
Crystal grow
*PLUS
Temperature: 4.0 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlprotein1drop
250 mMTris-HCl1drop
31 %(v/v)beta-mercaptoethanol1drop
41.8 Mammonium sulfate1reservoir
50.5 M1reservoirNaCl
60.1 MTris-HCl1reservoir
70.25 %BME1reservoir

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418
DetectorType: SIEMENS HI-STAR / Detector: AREA DETECTOR / Date: Apr 28, 1997
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2→20 Å / Num. obs: 16621 / % possible obs: 86 % / Observed criterion σ(I): 0 / Redundancy: 4.86 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 18.4
Reflection shellResolution: 2.008→2.081 Å / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 2 / % possible all: 38.6
Reflection
*PLUS
Num. measured all: 80685 / Rmerge(I) obs: 0.071
Reflection shell
*PLUS
% possible obs: 47.1 % / Rmerge(I) obs: 0.28

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Processing

Software
NameVersionClassification
XTAL3.0model building
SHELXL-97refinement
SADIEdata reduction
SAINTdata scaling
XTALV. 3.0phasing
RefinementMethod to determine structure: MIR / Resolution: 2→10 Å / σ(F): 4 / Stereochemistry target values: ENGH & HUBER /
RfactorNum. reflection
obs0.168 -
all-16400
Refine analyzeNum. disordered residues: 2
Refinement stepCycle: LAST / Resolution: 2→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1488 0 15 163 1666
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.03
X-RAY DIFFRACTIONs_angle_d0.2
X-RAY DIFFRACTIONs_similar_dist
X-RAY DIFFRACTIONs_from_restr_planes
X-RAY DIFFRACTIONs_zero_chiral_vol
X-RAY DIFFRACTIONs_non_zero_chiral_vol
X-RAY DIFFRACTIONs_anti_bump_dis_restr
X-RAY DIFFRACTIONs_rigid_bond_adp_cmpnt
X-RAY DIFFRACTIONs_similar_adp_cmpnt
X-RAY DIFFRACTIONs_approx_iso_adps
Software
*PLUS
Name: SHELXL-97 / Classification: refinement
Refinement
*PLUS
σ(F): 4 / Num. reflection Rfree: 661 / Rfactor all: 0.162 / Rfactor obs: 0.142 / Rfactor Rfree: 0.187
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONs_bond_d0.015
X-RAY DIFFRACTIONs_angle_d
X-RAY DIFFRACTIONs_angle_deg2.3

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