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- PDB-4bxq: Structure of the E1021V mutant of the TCP10 domain of Danio rerio CPAP -
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Open data
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Basic information
Entry | Database: PDB / ID: 4bxq | ||||||
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Title | Structure of the E1021V mutant of the TCP10 domain of Danio rerio CPAP | ||||||
![]() | CPAP | ||||||
![]() | CELL CYCLE / CENTRIOLE DUPLICATION | ||||||
Function / homology | ![]() TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / positive regulation of mitotic spindle organization / centriole elongation / procentriole replication complex / positive regulation of centriole replication / positive regulation of spindle assembly / cilium assembly / positive regulation of G1/S transition of mitotic cell cycle / centriole / tubulin binding ...TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain / positive regulation of mitotic spindle organization / centriole elongation / procentriole replication complex / positive regulation of centriole replication / positive regulation of spindle assembly / cilium assembly / positive regulation of G1/S transition of mitotic cell cycle / centriole / tubulin binding / protein domain specific binding / centrosome / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | van Breugel, M. | ||||||
![]() | ![]() Title: Crystal structures of the CPAP/STIL complex reveal its role in centriole assembly and human microcephaly. Authors: Cottee, M.A. / Muschalik, N. / Wong, Y.L. / Johnson, C.M. / Johnson, S. / Andreeva, A. / Oegema, K. / Lea, S.M. / Raff, J.W. / van Breugel, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51 KB | Display | ![]() |
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PDB format | ![]() | 35.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.1 KB | Display | ![]() |
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Full document | ![]() | 430.9 KB | Display | |
Data in XML | ![]() | 9.4 KB | Display | |
Data in CIF | ![]() | 12.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bxpSC ![]() 4bxrC ![]() 4by2C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21861.557 Da / Num. of mol.: 1 / Fragment: TCP-10 DOMAIN, RESIDUE 937-1124 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.6 % / Description: NONE |
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Crystal grow | pH: 8.5 Details: 80 MM TRIS PH 8.5, 160 MM MGCL2, 24% PEG-4000, 20% GLYCEROL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Nov 11, 2010 / Details: MULTILAYER FOCUSSING OPTICS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→36.5 Å / Num. obs: 15136 / % possible obs: 100 % / Observed criterion σ(I): 1.8 / Redundancy: 6.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 6.6 % / Rmerge(I) obs: 1.09 / Mean I/σ(I) obs: 1.8 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4BXP Resolution: 1.9→29.49 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.926 / SU B: 4.329 / SU ML: 0.124 / Cross valid method: THROUGHOUT / ESU R: 0.173 / ESU R Free: 0.168 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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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: 31.553 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→29.49 Å
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Refine LS restraints |
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