+Open data
-Basic information
Entry | Database: PDB / ID: 1nvs | ||||||
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Title | The Complex Structure Of Checkpoint Kinase Chk1/SB218078 | ||||||
Components |
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Keywords | TRANSFERASE / Chk1-SB218078 complex | ||||||
Function / homology | Function and homology information negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / Activation of ATR in response to replication stress / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination ...negative regulation of G0 to G1 transition / apoptotic process involved in development / histone H3T11 kinase activity / negative regulation of DNA biosynthetic process / mitotic G2/M transition checkpoint / negative regulation of mitotic nuclear division / regulation of mitotic centrosome separation / Activation of ATR in response to replication stress / inner cell mass cell proliferation / regulation of double-strand break repair via homologous recombination / negative regulation of gene expression, epigenetic / nucleus organization / cellular response to caffeine / Transcriptional Regulation by E2F6 / mitotic G2 DNA damage checkpoint signaling / Presynaptic phase of homologous DNA pairing and strand exchange / condensed nuclear chromosome / replicative senescence / signal transduction in response to DNA damage / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / positive regulation of cell cycle / regulation of signal transduction by p53 class mediator / DNA damage checkpoint signaling / replication fork / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / TP53 Regulates Transcription of DNA Repair Genes / peptidyl-threonine phosphorylation / G2/M DNA damage checkpoint / cellular response to mechanical stimulus / Signaling by SCF-KIT / G2/M transition of mitotic cell cycle / Processing of DNA double-strand break ends / regulation of cell population proliferation / DNA replication / Regulation of TP53 Activity through Phosphorylation / chromatin remodeling / non-specific serine/threonine protein kinase / protein kinase activity / protein domain specific binding / protein phosphorylation / intracellular membrane-bounded organelle / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / DNA damage response / chromatin / apoptotic process / protein-containing complex / extracellular space / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Zhao, B. / Bower, M.J. / McDevitt, P.J. / Zhao, H. / Davis, S.T. / Johanson, K.O. / Green, S.M. / Concha, N.O. / Zhou, B.B. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Structural Basis for Chk1 Inhibition by UCN-01 Authors: Zhao, B. / Bower, M.J. / McDevitt, P.J. / Zhao, H. / Davis, S.T. / Johanson, K.O. / Green, S.M. / Concha, N.O. / Zhou, B.B. | ||||||
History |
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Remark 999 | SEQUENCE A five-residue peptide 301-305 was found with the enzyme. Residues were named based on the ...SEQUENCE A five-residue peptide 301-305 was found with the enzyme. Residues were named based on the electron density. The peptide could be the part of C-terminal missing residues. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nvs.cif.gz | 72.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nvs.ent.gz | 52.5 KB | Display | PDB format |
PDBx/mmJSON format | 1nvs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nvs_validation.pdf.gz | 916.2 KB | Display | wwPDB validaton report |
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Full document | 1nvs_full_validation.pdf.gz | 920.8 KB | Display | |
Data in XML | 1nvs_validation.xml.gz | 14.6 KB | Display | |
Data in CIF | 1nvs_validation.cif.gz | 20.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nv/1nvs ftp://data.pdbj.org/pub/pdb/validation_reports/nv/1nvs | HTTPS FTP |
-Related structure data
Related structure data | 1nvqC 1nvrC 2phkS C: citing same article (ref.) S: Starting model for refinement |
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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: 33042.988 Da / Num. of mol.: 1 / Fragment: CHK1KD (RESIDUES 1-289) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: unidentified baculovirus / Strain (production host): sf9 References: UniProt: O14757, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor |
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#2: Protein/peptide | Mass: 433.457 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: Chemical | ChemComp-SO4 / |
#4: Chemical | ChemComp-UCM / |
#5: 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: 2.57 Å3/Da / Density % sol: 51.84 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: PEG8000, ammonium sulfate, glycerol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-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: Dec 2, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. all: 31508 / Num. obs: 31484 / % possible obs: 100 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 31954 / % possible obs: 99 % / Redundancy: 4.2 % / Num. measured all: 133128 / Rmerge(I) obs: 0.065 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2PHK Resolution: 1.8→20 Å / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 20 Å / % reflection Rfree: 6 % / Rfactor Rfree: 0.255 / Rfactor Rwork: 0.231 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.191 |