+Open data
-Basic information
Entry | Database: PDB / ID: 1ou5 | ||||||
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Title | Crystal structure of human CCA-adding enzyme | ||||||
Components | tRNA CCA-adding enzyme | ||||||
Keywords | TRANSLATION / TRANSFERASE / tRNA / polymerase / nucleotidyltransferase | ||||||
Function / homology | Function and homology information 5'-3' RNA polymerase activity / CCA tRNA nucleotidyltransferase activity / tRNA processing in the mitochondrion / mitochondrial tRNA 3'-end processing / tRNA surveillance / CCACCA tRNA nucleotidyltransferase activity / CCA tRNA nucleotidyltransferase / tRNA 3'-terminal CCA addition / tRNA 3'-end processing / tRNA processing in the nucleus ...5'-3' RNA polymerase activity / CCA tRNA nucleotidyltransferase activity / tRNA processing in the mitochondrion / mitochondrial tRNA 3'-end processing / tRNA surveillance / CCACCA tRNA nucleotidyltransferase activity / CCA tRNA nucleotidyltransferase / tRNA 3'-terminal CCA addition / tRNA 3'-end processing / tRNA processing in the nucleus / rescue of stalled ribosome / tRNA binding / mitochondrial matrix / protein homodimerization activity / mitochondrion / nucleoplasm / ATP binding / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SIR / Resolution: 3.4 Å | ||||||
Authors | Augustin, M.A. / Reichert, A.S. / Betat, H. / Huber, R. / Moerl, M. / Steegborn, C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Crystal Structure of the Human CCA-adding Enzyme: Insights into Template-independent Polymerization Authors: Augustin, M.A. / Reichert, A.S. / Betat, H. / Huber, R. / Moerl, M. / Steegborn, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ou5.cif.gz | 130.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ou5.ent.gz | 104.4 KB | Display | PDB format |
PDBx/mmJSON format | 1ou5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ou5_validation.pdf.gz | 442.8 KB | Display | wwPDB validaton report |
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Full document | 1ou5_full_validation.pdf.gz | 499 KB | Display | |
Data in XML | 1ou5_validation.xml.gz | 29.8 KB | Display | |
Data in CIF | 1ou5_validation.cif.gz | 41.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ou/1ou5 ftp://data.pdbj.org/pub/pdb/validation_reports/ou/1ou5 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 51225.145 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: hMtCCA / Plasmid: PET30EK-LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RP / References: UniProt: Q96Q11 |
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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: 4.02 Å3/Da / Density % sol: 69.2 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 100mM sodium citrate, 2.2M ammonium sulfate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 290K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 21, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.4→50 Å / Num. obs: 17609 / % possible obs: 98.9 % / Observed criterion σ(I): 1 / Redundancy: 2.7 % / Biso Wilson estimate: 78.9 Å2 / Rmerge(I) obs: 0.076 / Rsym value: 0.076 / Net I/σ(I): 9 |
Reflection shell | Resolution: 3.4→3.58 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.373 / Mean I/σ(I) obs: 2.1 / Num. unique all: 2373 / Rsym value: 0.373 / % possible all: 98.9 |
Reflection | *PLUS Lowest resolution: 25 Å / Num. obs: 17538 / % possible obs: 99.1 % / Num. measured all: 46729 / Rmerge(I) obs: 0.069 |
Reflection shell | *PLUS % possible obs: 98.9 % / Rmerge(I) obs: 0.273 / Mean I/σ(I) obs: 2.7 |
-Processing
Software |
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Refinement | Method to determine structure: SIR / Resolution: 3.4→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.4→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.4→3.486 Å
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Refinement | *PLUS Highest resolution: 3.4 Å / Lowest resolution: 20 Å | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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