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Yorodumi- PDB-4rlq: Crystal structure of a benzoate coenzyme A ligase with o-Toluic acid -
+Open data
-Basic information
Entry | Database: PDB / ID: 4rlq | ||||||
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Title | Crystal structure of a benzoate coenzyme A ligase with o-Toluic acid | ||||||
Components | Benzoate-coenzyme A ligase | ||||||
Keywords | LIGASE / Substrate Specificity / Kinetics | ||||||
Function / homology | Function and homology information acid-thiol ligase activity / CoA-ligase activity / secondary metabolite biosynthetic process / ATP binding Similarity search - Function | ||||||
Biological species | Rhodopseudomonas palustris (phototrophic) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.63 Å | ||||||
Authors | Strom, S. / Nosrati, M. / Thornburg, C. / Walker, K.D. / Geiger, J.H. | ||||||
Citation | Journal: Biochemistry / Year: 2015 Title: Kinetically and Crystallographically Guided Mutations of a Benzoate CoA Ligase (BadA) Elucidate Mechanism and Expand Substrate Permissivity. Authors: Thornburg, C.K. / Wortas-Strom, S. / Nosrati, M. / Geiger, J.H. / Walker, K.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4rlq.cif.gz | 221.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4rlq.ent.gz | 175.5 KB | Display | PDB format |
PDBx/mmJSON format | 4rlq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4rlq_validation.pdf.gz | 464.9 KB | Display | wwPDB validaton report |
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Full document | 4rlq_full_validation.pdf.gz | 474.3 KB | Display | |
Data in XML | 4rlq_validation.xml.gz | 43 KB | Display | |
Data in CIF | 4rlq_validation.cif.gz | 63.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/4rlq ftp://data.pdbj.org/pub/pdb/validation_reports/rl/4rlq | HTTPS FTP |
-Related structure data
Related structure data | 4eatC 4rlfC 4rm2C 4rm3C 4rmnC 4zjzC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 56333.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rhodopseudomonas palustris (phototrophic) Gene: badA / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / References: UniProt: Q93TK0 #2: Chemical | #3: Chemical | ChemComp-GOL / #4: 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: 2.27 Å3/Da / Density % sol: 45.91 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 15 % PEG 3350, 0.1 M Tris pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97872 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 16, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→50 Å / Num. all: 442714 / Num. obs: 115478 / % possible obs: 96.9 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.077 / Rsym value: 0.055 / Net I/σ(I): 17.1 |
Reflection shell | Resolution: 1.63→1.66 Å / Redundancy: 2 % / Rmerge(I) obs: 0.443 / Mean I/σ(I) obs: 1.35 / Rsym value: 0.44 / % possible all: 74.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.63→33.04 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.955 / SU B: 2.02 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.086 / ESU R Free: 0.088 / 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: 21.264 Å2
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Refinement step | Cycle: LAST / Resolution: 1.63→33.04 Å
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