+Open data
-Basic information
Entry | Database: PDB / ID: 5loh | |||||||||
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Title | Kinase domain of human Greatwall | |||||||||
Components | Serine/threonine-protein kinase greatwall,Serine/threonine-protein kinase greatwall | |||||||||
Keywords | TRANSFERASE / Kinase domain / Inhibitor | |||||||||
Function / homology | Function and homology information protein serine/threonine kinase activity => GO:0004674 / MASTL Facilitates Mitotic Progression / negative regulation of phosphoprotein phosphatase activity / cleavage furrow / protein phosphatase 2A binding / G2/M transition of mitotic cell cycle / mitotic cell cycle / kinase activity / peptidyl-serine phosphorylation / regulation of cell cycle ...protein serine/threonine kinase activity => GO:0004674 / MASTL Facilitates Mitotic Progression / negative regulation of phosphoprotein phosphatase activity / cleavage furrow / protein phosphatase 2A binding / G2/M transition of mitotic cell cycle / mitotic cell cycle / kinase activity / peptidyl-serine phosphorylation / regulation of cell cycle / non-specific serine/threonine protein kinase / intracellular signal transduction / cell division / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / DNA damage response / nucleoplasm / ATP binding / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | |||||||||
Authors | Rajasekaran, M.B. / Pearl, L.H. / Oliver, A.W. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: Oncotarget / Year: 2016 Title: A first generation inhibitor of human Greatwall kinase, enabled by structural and functional characterisation of a minimal kinase domain construct. Authors: Ocasio, C.A. / Rajasekaran, M.B. / Walker, S. / Le Grand, D. / Spencer, J. / Pearl, F.M. / Ward, S.E. / Savic, V. / Pearl, L.H. / Hochegger, H. / Oliver, A.W. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5loh.cif.gz | 116.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5loh.ent.gz | 87 KB | Display | PDB format |
PDBx/mmJSON format | 5loh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lo/5loh ftp://data.pdbj.org/pub/pdb/validation_reports/lo/5loh | HTTPS FTP |
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-Related structure data
Related structure data | 1h1wS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 38214.508 Da / Num. of mol.: 2 / Fragment: UNP residues 1-194,UNP residues 740-879 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MASTL, GW, GWL, THC2 / Plasmid: pTHREE-E / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta2 References: UniProt: Q96GX5, non-specific serine/threonine protein kinase #2: Chemical | #3: Chemical | ChemComp-CL / | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.32 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, sitting drop Details: 0.2 M ammonium citrate, 20% w/v polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 1.03667 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 23, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.03667 Å / Relative weight: 1 |
Reflection | Resolution: 3→48.05 Å / Num. obs: 13060 / % possible obs: 99.5 % / Redundancy: 4.5 % / CC1/2: 0.985 / Rmerge(I) obs: 0.182 / Net I/σ(I): 6.7 |
Reflection shell | Resolution: 3→3.18 Å / Redundancy: 4.6 % / Rmerge(I) obs: 1.286 / Mean I/σ(I) obs: 1.1 / CC1/2: 0.381 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1H1W Resolution: 3.1→48.05 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 0.23 / Phase error: 27.4
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→48.05 Å
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Refine LS restraints |
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LS refinement shell |
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