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Yorodumi- PDB-4loc: Structure of the carboxyl transferase domain from Rhizobium etli ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4loc | ||||||
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Title | Structure of the carboxyl transferase domain from Rhizobium etli pyruvate carboxylase with oxamate and biotin | ||||||
Components | Pyruvate carboxylase | ||||||
Keywords | LIGASE / TIM Barrel | ||||||
Function / homology | Function and homology information pyruvate carboxylase / pyruvate carboxylase activity / pyruvate metabolic process / gluconeogenesis / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Rhizobium etli (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.26 Å | ||||||
Authors | Lietzan, A.D. / St.Maurice, M. | ||||||
Citation | Journal: Arch.Biochem.Biophys. / Year: 2014 Title: The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase. Authors: Lietzan, A.D. / Lin, Y. / St.Maurice, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4loc.cif.gz | 912.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4loc.ent.gz | 755.9 KB | Display | PDB format |
PDBx/mmJSON format | 4loc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lo/4loc ftp://data.pdbj.org/pub/pdb/validation_reports/lo/4loc | HTTPS FTP |
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-Related structure data
Related structure data | 4m6vC 4jx4S S: Starting model for refinement C: citing same article (ref.) |
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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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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 69963.375 Da / Num. of mol.: 4 Fragment: Carboxyl transferase domain, UNP residues 465-1067 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhizobium etli (bacteria) / Strain: CFN 42 / Gene: pyc, RHE_CH04002 / Plasmid: pET-28a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q2K340, pyruvate carboxylase |
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-Non-polymers , 7 types, 556 molecules
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-MG / #4: Chemical | #5: Chemical | ChemComp-BTN / #6: Chemical | ChemComp-OXM / #7: Chemical | #8: 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: 2.88 Å3/Da / Density % sol: 57.3 % |
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Crystal grow | Temperature: 298 K / Method: batch crystallization under oil / pH: 6 Details: 14% (w/v) PEG 8000, 110 mM MOPS (pH 6.0), 165 mM Tetramethylammonium chloride, 2% (v/v) glycerol, BATCH CRYSTALLIZATION UNDER OIL, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jul 18, 2011 |
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 2.26→50 Å / Num. all: 148360 / Num. obs: 145868 / % possible obs: 98.3 % / Observed criterion σ(I): -3 / Redundancy: 7.1 % / Biso Wilson estimate: 34.4 Å2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.26→2.3 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.444 / Mean I/σ(I) obs: 3.4 / % possible all: 94.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4JX4 Resolution: 2.26→43.75 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.941 / SU B: 9.969 / SU ML: 0.126 / Cross valid method: THROUGHOUT / ESU R: 0.216 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 50.934 Å2
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Refinement step | Cycle: LAST / Resolution: 2.26→43.75 Å
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Refine LS restraints |
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