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Yorodumi- PDB-4mfe: Structure of the carboxyl transferase domain from Rhizobium etli ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4mfe | ||||||
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Title | Structure of the carboxyl transferase domain from Rhizobium etli pyruvate carboxylase with 3-hydroxypyruvate | ||||||
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: 2.61 Å | ||||||
Authors | Lietzan, A.D. / St.Maurice, M. | ||||||
Citation | Journal: Biochem.Biophys.Res.Commun. / Year: 2013 Title: Insights into the carboxyltransferase reaction of pyruvate carboxylase from the structures of bound product and intermediate analogs. Authors: Lietzan, A.D. / 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 | 4mfe.cif.gz | 900.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4mfe.ent.gz | 746.6 KB | Display | PDB format |
PDBx/mmJSON format | 4mfe.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4mfe_validation.pdf.gz | 525.6 KB | Display | wwPDB validaton report |
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Full document | 4mfe_full_validation.pdf.gz | 556.2 KB | Display | |
Data in XML | 4mfe_validation.xml.gz | 82.5 KB | Display | |
Data in CIF | 4mfe_validation.cif.gz | 112.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mf/4mfe ftp://data.pdbj.org/pub/pdb/validation_reports/mf/4mfe | HTTPS FTP |
-Related structure data
Related structure data | 4mfdC 4mimC 4jx4S C: citing same article (ref.) S: Starting model for refinement |
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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, 190 molecules
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-3PY / #4: Chemical | ChemComp-BTN / #5: Chemical | ChemComp-MG / #6: Chemical | #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: 2.89 Å3/Da / Density % sol: 57.45 % |
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Crystal grow | Temperature: 298 K / Method: batch crystallization under oil / pH: 6 Details: 11.3% (w/v) PEG 8000, 99 mM BisTris, 346 mM tetramethylammonium chloride, pH 6.0, 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: 0.979 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 22, 2011 |
Radiation | Monochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. all: 95807 / Num. obs: 91812 / % possible obs: 96 % / Observed criterion σ(I): -3 / Redundancy: 5.5 % / Biso Wilson estimate: 59.9 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 22.8 |
Reflection shell | Resolution: 2.6→2.64 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.434 / Mean I/σ(I) obs: 3.3 / % possible all: 93.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4JX4 Resolution: 2.61→49.37 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.941 / SU B: 17.624 / SU ML: 0.185 / Cross valid method: THROUGHOUT / ESU R: 0.45 / ESU R Free: 0.267 / 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: 74.213 Å2
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Refinement step | Cycle: LAST / Resolution: 2.61→49.37 Å
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Refine LS restraints |
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