+Open data
-Basic information
Entry | Database: PDB / ID: 1tau | ||||||
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Title | TAQ POLYMERASE (E.C.2.7.7.7)/DNA/B-OCTYLGLUCOSIDE COMPLEX | ||||||
Components |
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Keywords | transferase/DNA / PROTEIN-DNA COMPLEX / Taq DNA Polymerase / transferase-DNA COMPLEX | ||||||
Function / homology | Function and homology information nucleoside binding / hydrolase activity, acting on ester bonds / double-strand break repair via alternative nonhomologous end joining / DNA-templated DNA replication / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA binding Similarity search - Function | ||||||
Biological species | Thermus aquaticus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å | ||||||
Authors | Eom, S.H. / Wang, J. / Steitz, T.A. | ||||||
Citation | Journal: Nature / Year: 1996 Title: Structure of Taq ploymerase with DNA at the polymerase active site. Authors: Eom, S.H. / Wang, J. / Steitz, T.A. #1: Journal: Nature / Year: 1995 Title: Crystal Structure of Thermus Aquatics DNA Polymerase Authors: Kim, Y. / Eom, S.H. / Wang, J. / Lee, D.-S. / Suh, S.W. / Steitz, T.A. #2: Journal: J.Biol.Chem. / Year: 1989 Title: Isolation, Characterization, and Expression in Escherichia Coli of the DNA Polymerase Gene From Thermus Aquaticus Authors: Lawyer, F.C. / Stoffel, S. / Saiki, R.K. / Myambo, K. / Drummond, R. / Gelfand, D.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tau.cif.gz | 208.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tau.ent.gz | 162.5 KB | Display | PDB format |
PDBx/mmJSON format | 1tau.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tau_validation.pdf.gz | 637.6 KB | Display | wwPDB validaton report |
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Full document | 1tau_full_validation.pdf.gz | 686.5 KB | Display | |
Data in XML | 1tau_validation.xml.gz | 35 KB | Display | |
Data in CIF | 1tau_validation.cif.gz | 47.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ta/1tau ftp://data.pdbj.org/pub/pdb/validation_reports/ta/1tau | 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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Unit cell |
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-Components
#1: DNA chain | Mass: 2427.605 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#2: DNA chain | Mass: 2427.605 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: Protein | Mass: 94046.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus aquaticus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P19821, DNA-directed DNA polymerase |
#4: Sugar | ChemComp-BGL / |
#5: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57.06 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6 Details: pH 6.00, VAPOR DIFFUSION, HANGING DROP, temperature 295.00K | ||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal | *PLUS Density % sol: 50 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 6 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1995 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3→50 Å / Num. obs: 21866 / % possible obs: 93.3 % / Observed criterion σ(I): 3 / Rmerge(I) obs: 0.088 / Net I/σ(I): 8.9 |
Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 50 Å / % possible obs: 93.3 % / Observed criterion σ(I): 3 |
-Processing
Software |
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Refinement | Resolution: 3→8 Å / σ(F): 3
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Displacement parameters | Biso mean: 45 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 8 Å / σ(F): 3 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 45 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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