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Open data
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Basic information
Entry | Database: PDB / ID: 5dgo | ||||||
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Title | Crystal structure of cell division cycle protein 45 (Cdc45) | ||||||
![]() | Cell division control protein 45 homolog | ||||||
![]() | CELL CYCLE / DNA replication / CMG helicase subunit / RecJ fold | ||||||
Function / homology | ![]() Unwinding of DNA / mitotic DNA replication preinitiation complex assembly / CMG complex / DNA replication checkpoint signaling / DNA replication preinitiation complex / double-strand break repair via break-induced replication / G1/S-Specific Transcription / DNA unwinding involved in DNA replication / DNA replication origin binding / Activation of the pre-replicative complex ...Unwinding of DNA / mitotic DNA replication preinitiation complex assembly / CMG complex / DNA replication checkpoint signaling / DNA replication preinitiation complex / double-strand break repair via break-induced replication / G1/S-Specific Transcription / DNA unwinding involved in DNA replication / DNA replication origin binding / Activation of the pre-replicative complex / DNA replication initiation / Activation of ATR in response to replication stress / ciliary basal body / single-stranded DNA binding / centrosome / chromatin binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Simon, A.C. / Pellegrini, L. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of human Cdc45 and implications for CMG helicase function. Authors: Simon, A.C. / Sannino, V. / Costanzo, V. / Pellegrini, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 235.1 KB | Display | ![]() |
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PDB format | ![]() | 198.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.2 KB | Display | ![]() |
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Full document | ![]() | 441.6 KB | Display | |
Data in XML | ![]() | 26.2 KB | Display | |
Data in CIF | ![]() | 40.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 64277.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Residues 154 to 164 (11 aminoacids) were left out of the expression construct used for determination of the crystal structure. Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-EDO / #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.09 Å3/Da / Density % sol: 69.91 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop Details: Buffer condition C2 of the Morpheus HT 96 crystallisation screen (Molecular Dimensions) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 28, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9778 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→48.84 Å / Num. obs: 61965 / % possible obs: 99.8 % / Redundancy: 6.6 % / Biso Wilson estimate: 33.7 Å2 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 2.1→2.15 Å / Redundancy: 6.5 % / Rmerge(I) obs: 1.042 / Mean I/σ(I) obs: 2.1 / % possible all: 97.1 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 43.8 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→48.84 Å
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Refine LS restraints |
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LS refinement shell |
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