+Open data
-Basic information
Entry | Database: PDB / ID: 1zt2 | ||||||
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Title | Heterodimeric structure of the core primase. | ||||||
Components |
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Keywords | replication / transferase / Heterodimeric complex | ||||||
Function / homology | Function and homology information primosome complex / DNA primase activity / DNA replication, synthesis of primer / DNA-directed RNA polymerase complex / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / 4 iron, 4 sulfur cluster binding / metal ion binding Similarity search - Function | ||||||
Biological species | Sulfolobus solfataricus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.33 Å | ||||||
Authors | Lao-Sirieix, S.H. / Nookala, R.K. / Roversi, P. / Bell, S.D. / Pellegrini, L. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2005 Title: Structure of the heterodimeric core primase. Authors: Lao-Sirieix, S.H. / Nookala, R.K. / Roversi, P. / Bell, S.D. / Pellegrini, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zt2.cif.gz | 223.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zt2.ent.gz | 187.6 KB | Display | PDB format |
PDBx/mmJSON format | 1zt2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1zt2_validation.pdf.gz | 489.3 KB | Display | wwPDB validaton report |
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Full document | 1zt2_full_validation.pdf.gz | 548.4 KB | Display | |
Data in XML | 1zt2_validation.xml.gz | 46.3 KB | Display | |
Data in CIF | 1zt2_validation.cif.gz | 61.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zt/1zt2 ftp://data.pdbj.org/pub/pdb/validation_reports/zt/1zt2 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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5 |
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Unit cell |
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Details | The biological assembly is a heterodimer of two chains. One heterodimer is formed by chains A and B, and another heterodimer is formed by chains C and D. There are therefore two copies of the biological assembly in the asimmetric unit. |
-Components
#1: Protein | Mass: 37643.895 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Gene: priA / Plasmid: pET-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE) References: UniProt: Q97Z83, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #2: Protein | Mass: 24906.250 Da / Num. of mol.: 2 / Fragment: residues 1-212 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Gene: priB / Plasmid: pET-Duet / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE) References: UniProt: Q9UWW1, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases #3: Chemical | #4: Chemical | ChemComp-SO4 / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: Tris hydrochloride, Ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.28242 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: May 10, 2004 |
Radiation | Monochromator: Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.28242 Å / Relative weight: 1 |
Reflection | Resolution: 3.33→39.12 Å / Num. all: 59500 / Num. obs: 59500 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 12 % / Rsym value: 0.133 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 3.33→3.47 Å / Redundancy: 12.2 % / Mean I/σ(I) obs: 2.1 / Num. unique all: 5825 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 3.33→39.12 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 89.922 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.33→39.12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.33→3.43 Å / Rfactor Rfree: 0.279 / Rfactor Rwork: 0.281 |