+Open data
-Basic information
Entry | Database: PDB / ID: 4mm2 | ||||||
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Title | Crystal structure of yeast primase catalytic subunit | ||||||
Components | DNA primase small subunitPrimase | ||||||
Keywords | REPLICATION / zinc finger | ||||||
Function / homology | Function and homology information Inhibition of replication initiation of damaged DNA by RB1/E2F1 / DNA replication initiation / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching / alpha DNA polymerase:primase complex / Activation of the pre-replicative complex / DNA primase activity / DNA replication, synthesis of primer / nuclear replication fork ...Inhibition of replication initiation of damaged DNA by RB1/E2F1 / DNA replication initiation / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching / alpha DNA polymerase:primase complex / Activation of the pre-replicative complex / DNA primase activity / DNA replication, synthesis of primer / nuclear replication fork / DNA replication initiation / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / DNA replication / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Park, K.R. / An, J.Y. / Lee, Y. / Youn, H.S. / Lee, J.G. / Kang, J.Y. / Kim, T.G. / Lim, J.J. / Eom, S.H. / Wang, J. | ||||||
Citation | Journal: To be Published Title: Crystal structure of yeast primase catalytic subunit Authors: Park, K.R. / An, J.Y. / Lee, Y. / Youn, H.S. / Lee, J.G. / Kang, J.Y. / Kim, T.G. / Lim, J.J. / Eom, S.H. / Wang, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4mm2.cif.gz | 185.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mm2.ent.gz | 145.6 KB | Display | PDB format |
PDBx/mmJSON format | 4mm2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mm/4mm2 ftp://data.pdbj.org/pub/pdb/validation_reports/mm/4mm2 | HTTPS FTP |
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-Related structure data
Related structure data | 4mhqS S: Starting model for refinement |
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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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: PRO / Beg label comp-ID: PRO / End auth comp-ID: ASP / End label comp-ID: ASP / Refine code: 0 / Auth seq-ID: 10 - 402 / Label seq-ID: 15 - 407
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-Components
#1: Protein | Mass: 48163.824 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Strain: ATCC 204508 / S288c / Gene: PRI1, YIR008C, YIB8C / Plasmid: pETDuet vector / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P10363, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #2: Chemical | ChemComp-CD / #3: Chemical | #4: 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: 2.41 Å3/Da / Density % sol: 49.02 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 5.5 Details: 0.1M Na-Citrate, 0.2M NDSB, 5mM CdCl2, 30% PEG 600, 10mM ZnCl2 , pH 5.5, VAPOR DIFFUSION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1.2826 Å |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD |
Radiation | Monochromator: Numerical link type Si(111) double crystal monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.2826 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→50 Å / Num. all: 111075 / Num. obs: 111075 / % possible obs: 92.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.6 % / Rmerge(I) obs: 0.108 / Net I/σ(I): 10.17 |
Reflection shell | Resolution: 1.6→1.64 Å / Redundancy: 3.6 % / Rmerge(I) obs: 1.988 / Mean I/σ(I) obs: 0.89 / Num. unique all: 5296 / % possible all: 59.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4MHQ Resolution: 1.6→43.88 Å / Cor.coef. Fo:Fc: 0.92 / Cor.coef. Fo:Fc free: 0.891 / SU B: 3.518 / SU ML: 0.119 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.129 / ESU R Free: 0.127 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 28.749 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→43.88 Å
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Refine LS restraints |
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