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Open data
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Basic information
Entry | Database: PDB / ID: 7pt5 | ||||||
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Title | Crystal structure of the CH domain of human CEP44 | ||||||
![]() | Centrosomal protein of 44 kDa | ||||||
![]() | CELL CYCLE / Centriole / Centrosome / Microtubule-associated protein | ||||||
Function / homology | ![]() centriole-centriole cohesion / centrosome cycle / centriole replication / centriole / spindle pole / midbody / microtubule binding / centrosome / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rosa e Silva, I. / van Breugel, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural validation and assessment of AlphaFold2 predictions for centrosomal and centriolar proteins and their complexes. Authors: van Breugel, M. / Rosa E Silva, I. / Andreeva, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 72.2 KB | Display | ![]() |
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PDB format | ![]() | 47.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 422.3 KB | Display | ![]() |
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Full document | ![]() | 423.1 KB | Display | |
Data in XML | ![]() | 6.4 KB | Display | |
Data in CIF | ![]() | 7.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7ptbC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 16753.955 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: amino acid residues GAMDP are residues of TEV protease cleavage Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.71 % |
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Crystal grow | Temperature: 292.15 K / Method: vapor diffusion Details: 100 nl protein solution and 100 nl of reservoir solution which was 0.1 M Hepes pH 7.3, 10% isopropanol, 10% PEG-4000. Crystals were mounted 0.1 M Hepes pH 7.5, 7.5% isopropanol, 30% PEG-400. |
-Data collection
Diffraction | Mean temperature: 80 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jun 23, 2018 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97928 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→81.1 Å / Num. obs: 7159 / % possible obs: 100 % / Redundancy: 21.4 % / Biso Wilson estimate: 73.06 Å2 / Rmerge(I) obs: 0.084 / Rpim(I) all: 0.019 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 2.3→2.38 Å / Mean I/σ(I) obs: 1.9 / Num. unique obs: 661 / Rpim(I) all: 0.506 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 103.08 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→33.62 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 6.58776806038 Å / Origin y: 24.0539816559 Å / Origin z: 14.266926446 Å
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Refinement TLS group | Selection details: { A|* } |