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Yorodumi- PDB-5lhz: PB3 Domain of Human PLK4 in Complex with Coiled-Coil Domain of STIL -
+Open data
-Basic information
Entry | Database: PDB / ID: 5lhz | |||||||||
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Title | PB3 Domain of Human PLK4 in Complex with Coiled-Coil Domain of STIL | |||||||||
Components |
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Keywords | STRUCTURAL PROTEIN / Polo box domain / Centriole / Complex / transferase | |||||||||
Function / homology | Function and homology information floor plate development / de novo centriole assembly involved in multi-ciliated epithelial cell differentiation / procentriole / deuterosome / regulation of centriole replication / procentriole replication complex / positive regulation of centriole replication / trophoblast giant cell differentiation / embryonic axis specification / positive regulation of spindle assembly ...floor plate development / de novo centriole assembly involved in multi-ciliated epithelial cell differentiation / procentriole / deuterosome / regulation of centriole replication / procentriole replication complex / positive regulation of centriole replication / trophoblast giant cell differentiation / embryonic axis specification / positive regulation of spindle assembly / notochord development / polo kinase / XY body / determination of left/right symmetry / protein localization to centrosome / neural tube development / smoothened signaling pathway / heart looping / centriole replication / cleavage furrow / centrosome duplication / cilium assembly / positive regulation of G1/S transition of mitotic cell cycle / regulation of mitotic spindle organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / forebrain development / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / centriole / AURKA Activation by TPX2 / mitotic spindle organization / neural tube closure / multicellular organism growth / kinetochore / spindle pole / Regulation of PLK1 Activity at G2/M Transition / cell cortex / in utero embryonic development / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / nucleolus / negative regulation of apoptotic process / nucleoplasm / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.51 Å | |||||||||
Authors | Cottee, M.A. / Lea, S.M. | |||||||||
Funding support | United Kingdom, 2items
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Citation | Journal: Biol Open / Year: 2017 Title: A key centriole assembly interaction interface between human PLK4 and STIL appears to not be conserved in flies. Authors: Cottee, M.A. / Johnson, S. / Raff, J.W. / Lea, S.M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5lhz.cif.gz | 121.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5lhz.ent.gz | 96.5 KB | Display | PDB format |
PDBx/mmJSON format | 5lhz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5lhz_validation.pdf.gz | 465.6 KB | Display | wwPDB validaton report |
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Full document | 5lhz_full_validation.pdf.gz | 466.4 KB | Display | |
Data in XML | 5lhz_validation.xml.gz | 11.4 KB | Display | |
Data in CIF | 5lhz_validation.cif.gz | 15 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lh/5lhz ftp://data.pdbj.org/pub/pdb/validation_reports/lh/5lhz | HTTPS FTP |
-Related structure data
Related structure data | 5lhwC 5lhxC 5lhyC 4yypS 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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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 9915.191 Da / Num. of mol.: 3 / Fragment: UNP residues 884-970 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PLK4, SAK, STK18 / Production host: Escherichia coli B (bacteria) / Strain (production host): B834 / References: UniProt: O00444, polo kinase #2: Protein/peptide | Mass: 3199.662 Da / Num. of mol.: 3 / Fragment: UNP residues 726-750 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: STIL, SIL / Production host: Escherichia coli B (bacteria) / Strain (production host): C41 / References: UniProt: Q15468 #3: 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: 2.36 Å3/Da / Density % sol: 47.78 % / Description: Hexagonal rod |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 150nl Protein solution (41.87 mg/ml protein in 20 mM Tris pH 7.5, 150 mM NaCl, 2 mM DTT) and 50 nl mother liquor (100mM MES pH 6.0, 191.7 mM Zn acetate, 10% Isopropanol) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 30, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.51→36.223 Å / Num. obs: 13265 / % possible obs: 99.7 % / Redundancy: 6.2 % / CC1/2: 0.995 / Net I/σ(I): 12.1 |
Reflection shell | Highest resolution: 2.51 Å / Rmerge(I) obs: 1.312 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Model based on 4YYP Resolution: 2.51→36.223 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 32.21
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.51→36.223 Å
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Refine LS restraints |
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LS refinement shell |
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