+Open data
-Basic information
Entry | Database: PDB / ID: 6flj | ||||||
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Title | Crystal structure of Cep120 C2A_K76A mutant | ||||||
Components | Centrosomal protein of 120 kDaCentrosome | ||||||
Keywords | STRUCTURAL PROTEIN / Centriole / microtubule / Cep120 / C2 domain | ||||||
Function / homology | Function and homology information positive regulation of centriole elongation / positive regulation of establishment of protein localization / interkinetic nuclear migration / positive regulation of centrosome duplication / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development ...positive regulation of centriole elongation / positive regulation of establishment of protein localization / interkinetic nuclear migration / positive regulation of centrosome duplication / astral microtubule organization / positive regulation of cilium assembly / centrosome cycle / centriole / neurogenesis / cerebral cortex development / centrosome / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.751 Å | ||||||
Authors | Sharma, A. / Gerard, S.F. / Olieric, N. / Steinmetz, M.O. | ||||||
Citation | Journal: J. Struct. Biol. / Year: 2018 Title: Cep120 promotes microtubule formation through a unique tubulin binding C2 domain. Authors: Sharma, A. / Gerard, S.F. / Olieric, N. / Steinmetz, M.O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6flj.cif.gz | 91.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6flj.ent.gz | 70.8 KB | Display | PDB format |
PDBx/mmJSON format | 6flj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fl/6flj ftp://data.pdbj.org/pub/pdb/validation_reports/fl/6flj | HTTPS FTP |
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-Related structure data
Related structure data | 6flkC 4icwS 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: 17356.936 Da / Num. of mol.: 1 / Mutation: K76A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CEP120, CCDC100 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8N960 |
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#2: 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: 2.02 Å3/Da / Density % sol: 39.03 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 20% PEG 3350 and 0.2 M NaSCN |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: May 17, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→40.71 Å / Num. obs: 14678 / % possible obs: 99.92 % / Redundancy: 12.7 % / Biso Wilson estimate: 28.79 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.0688 / Rpim(I) all: 0.01999 / Rrim(I) all: 0.07171 / Net I/σ(I): 24.44 |
Reflection shell | Resolution: 1.751→1.814 Å / Redundancy: 12.2 % / Rmerge(I) obs: 1.925 / Mean I/σ(I) obs: 1.29 / Num. unique obs: 1425 / CC1/2: 0.712 / Rpim(I) all: 0.5672 / % possible all: 99.65 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4ICW Resolution: 1.751→40.71 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 28.36
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.751→40.71 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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