+Open data
-Basic information
Entry | Database: PDB / ID: 2in6 | ||||||
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Title | Wee1 kinase complex with inhibitor PD311839 | ||||||
Components | Wee1-like protein kinase | ||||||
Keywords | TRANSFERASE / protein-inhibitor complex | ||||||
Function / homology | Function and homology information G2/M DNA replication checkpoint / negative regulation of G2/M transition of mitotic cell cycle / Polo-like kinase mediated events / Cyclin E associated events during G1/S transition / negative regulation of G1/S transition of mitotic cell cycle / establishment of cell polarity / positive regulation of DNA replication / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex ...G2/M DNA replication checkpoint / negative regulation of G2/M transition of mitotic cell cycle / Polo-like kinase mediated events / Cyclin E associated events during G1/S transition / negative regulation of G1/S transition of mitotic cell cycle / establishment of cell polarity / positive regulation of DNA replication / Cyclin A/B1/B2 associated events during G2/M transition / Cyclin A:Cdk2-associated events at S phase entry / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / neuron projection morphogenesis / non-specific protein-tyrosine kinase / non-membrane spanning protein tyrosine kinase activity / G2/M transition of mitotic cell cycle / microtubule cytoskeleton organization / Factors involved in megakaryocyte development and platelet production / protein tyrosine kinase activity / cell division / nucleolus / magnesium ion binding / nucleoplasm / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Squire, C.J. / Dickson, J.M. / Ivanovic, I. / Baker, E.N. | ||||||
Citation | Journal: Eur.J.Med.Chem. / Year: 2008 Title: Synthesis and structure-activity relationships of N-6 substituted analogues of 9-hydroxy-4-phenylpyrrolo[3,4-c]carbazole-1,3(2H,6H)-diones as inhibitors of Wee1 and Chk1 checkpoint kinases. Authors: Smaill, J.B. / Baker, E.N. / Booth, R.J. / Bridges, A.J. / Dickson, J.M. / Dobrusin, E.M. / Ivanovic, I. / Kraker, A.J. / Lee, H.H. / Lunney, E.A. / Ortwine, D.F. / Palmer, B.D. / Quin, J. / ...Authors: Smaill, J.B. / Baker, E.N. / Booth, R.J. / Bridges, A.J. / Dickson, J.M. / Dobrusin, E.M. / Ivanovic, I. / Kraker, A.J. / Lee, H.H. / Lunney, E.A. / Ortwine, D.F. / Palmer, B.D. / Quin, J. / Squire, C.J. / Thompson, A.M. / Denny, W.A. #1: Journal: Structure / Year: 2005 Title: Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation. Authors: Squire, C.J. / Dickson, J.M. / Ivanovic, I. / Baker, E.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2in6.cif.gz | 68.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2in6.ent.gz | 49.1 KB | Display | PDB format |
PDBx/mmJSON format | 2in6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2in6_validation.pdf.gz | 788.2 KB | Display | wwPDB validaton report |
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Full document | 2in6_full_validation.pdf.gz | 794.1 KB | Display | |
Data in XML | 2in6_validation.xml.gz | 13.2 KB | Display | |
Data in CIF | 2in6_validation.cif.gz | 17.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/in/2in6 ftp://data.pdbj.org/pub/pdb/validation_reports/in/2in6 | HTTPS FTP |
-Related structure data
Related structure data | 2io6C 1x8bS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 32368.832 Da / Num. of mol.: 1 / Fragment: kinase domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: WEE1 / Plasmid: pFASTBacHTa / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF9 References: UniProt: P30291, non-specific protein-tyrosine kinase |
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#2: Chemical | ChemComp-839 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58.03 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: HEPES, sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 28, 2002 / Details: Pt/Pd ULE mirrors |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.89→50 Å / Num. all: 29232 / Num. obs: 29232 / % possible obs: 92.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.9 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 24 |
Reflection shell | Resolution: 1.89→1.96 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.329 / Mean I/σ(I) obs: 2.1 / Num. unique all: 2204 / % possible all: 71.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1X8B Resolution: 1.9→50 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.889 / SU B: 3.529 / SU ML: 0.106 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.166 / ESU R Free: 0.165 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.326 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.949 Å / Total num. of bins used: 20
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