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Yorodumi- PDB-6lrh: Crystal Structure of the Binary Complex of AgrE C264A mutant with... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6lrh | ||||||
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Title | Crystal Structure of the Binary Complex of AgrE C264A mutant with L-arginine | ||||||
Components | Alr4995 protein | ||||||
Keywords | HYDROLASE / arginine dihydrolase / bifunctional enzyme / GME family | ||||||
Function / homology | Function and homology information LOR/SDH bifunctional enzyme, conserved domain superfamily / : / : / Arginine dihydrolase ArgZ-like, C-terminal, Rossmann fold / Arginine dihydrolase ArgZ-like, C-terminal, first region / Conserved hypothetical protein CHP00300 / LOR/SDH bifunctional enzyme, conserved domain / LOR/SDH bifunctional enzyme conserved region / N,N dimethylarginine dimethylhydrolase, eukaryotic / Arginine deiminase Similarity search - Domain/homology | ||||||
Biological species | Nostoc sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.70510472826 Å | ||||||
Authors | Lee, H. / Rhee, S. | ||||||
Funding support | Korea, Republic Of, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2020 Title: Structural and mutational analyses of the bifunctional arginine dihydrolase and ornithine cyclodeaminase AgrE from the cyanobacteriumAnabaena. Authors: Lee, H. / Rhee, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6lrh.cif.gz | 327 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6lrh.ent.gz | 213 KB | Display | PDB format |
PDBx/mmJSON format | 6lrh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lr/6lrh ftp://data.pdbj.org/pub/pdb/validation_reports/lr/6lrh | HTTPS FTP |
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-Related structure data
Related structure data | 6lrfSC 6lrgC 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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-Components
#1: Protein | Mass: 78035.156 Da / Num. of mol.: 2 / Mutation: C264A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) (bacteria) Strain: PCC 7120 / SAG 25.82 / UTEX 2576 / Gene: alr4995 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8YMD9 #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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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: 2.97 Å3/Da / Density % sol: 58.58 % |
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Crystal grow | Temperature: 295.15 K / Method: vapor diffusion Details: sodium acetate, sodium citrate (pH5.5), PEG4000, glycerol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PAL/PLS / Beamline: 11C / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 29, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. obs: 50860 / % possible obs: 99.8 % / Redundancy: 6.6 % / Biso Wilson estimate: 33.688112406 Å2 / CC1/2: 0.941 / Net I/σ(I): 7.53 |
Reflection shell | Resolution: 2.7→2.8 Å / Num. unique obs: 5040 / CC1/2: 0.529 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6LRF Resolution: 2.70510472826→49.458 Å / SU ML: 0.272673135983 / Cross valid method: FREE R-VALUE / σ(F): 1.33377365093 / Phase error: 23.803518733
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.9775154861 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.70510472826→49.458 Å
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Refine LS restraints |
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LS refinement shell |
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