+Open data
-Basic information
Entry | Database: PDB / ID: 1ort | ||||||
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Title | ORNITHINE TRANSCARBAMOYLASE FROM PSEUDOMONAS AERUGINOSA | ||||||
Components | ORNITHINE TRANSCARBAMOYLASE | ||||||
Keywords | TRANSFERASE / ORNITHINE | ||||||
Function / homology | Function and homology information arginine deiminase pathway / ornithine carbamoyltransferase / ornithine carbamoyltransferase activity / citrulline biosynthetic process / arginine biosynthetic process via ornithine / arginine catabolic process to ornithine / amino acid binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Villeret, V. / Dideberg, O. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1995 Title: Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase family. Authors: Villeret, V. / Tricot, C. / Stalon, V. / Dideberg, O. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ort.cif.gz | 759.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ort.ent.gz | 632.7 KB | Display | PDB format |
PDBx/mmJSON format | 1ort.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ort_validation.pdf.gz | 456.5 KB | Display | wwPDB validaton report |
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Full document | 1ort_full_validation.pdf.gz | 680.5 KB | Display | |
Data in XML | 1ort_validation.xml.gz | 104.7 KB | Display | |
Data in CIF | 1ort_validation.cif.gz | 100.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/or/1ort ftp://data.pdbj.org/pub/pdb/validation_reports/or/1ort | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Details | THE ORNITHINE CARBAMOYLTRANSFERASE IS A DODECAMER COMPOSED OF TWELVE MONOMERS RELATED BY THE 23 POINT GROUP SYMMETRY. THE DEPOSITOR PROVIDED COORDINATES CORRESPONDING TO ONE MONOMER. THE DODECAMER WAS GENERATED BY THE PDB USING THE NON-CRYSTALLOGRAPHIC SYMMETRY ROTATION MATRICES PROVIDED BY THE DEPOSITOR. |
-Components
#1: Protein | Mass: 37958.250 Da / Num. of mol.: 12 / Mutation: E105G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / References: UniProt: P08308, ornithine carbamoyltransferase Compound details | THE STRUCTURE IS NOT THE NATIVE ENZYME BUT A MUTANT FORM IN WHICH THE GLUTAMATE 105 HAS BEEN ...THE STRUCTURE IS NOT THE NATIVE ENZYME BUT A MUTANT FORM IN WHICH THE GLUTAMATE 105 HAS BEEN REPLACED BY A GLYCINE. THIS MUTANT IS BLOCKED IN THE R STATE CONFORMATI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.07 Å3/Da / Density % sol: 60.04 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.0 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 294 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Jan 20, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. obs: 92630 / % possible obs: 85 % / Observed criterion σ(I): 3 / Redundancy: 1.2 % / Rmerge(I) obs: 0.05 |
Reflection | *PLUS Num. measured all: 116334 |
-Processing
Software |
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Refinement | Resolution: 3→5.5 Å / σ(F): 3 /
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Displacement parameters | Biso mean: 29 Å2 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→5.5 Å
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Xplor file |
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Software | *PLUS Name: X-PLOR / Classification: refinement | |||||||||||||||
Refinement | *PLUS | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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