[English] 日本語
Yorodumi- PDB-2qvy: 4-Chlorobenzoyl-CoA Ligase/Synthetase, I303G mutation, bound to 3... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2qvy | ||||||
---|---|---|---|---|---|---|---|
Title | 4-Chlorobenzoyl-CoA Ligase/Synthetase, I303G mutation, bound to 3,4-Dichlorobenzoate | ||||||
Components | 4-Chlorobenzoate CoA Ligase | ||||||
Keywords | LIGASE / Adenylate-forming enzymes / Acyl-CoA ligase | ||||||
Function / homology | Function and homology information medium-chain fatty acid-CoA ligase activity / fatty acid metabolic process / nucleotide binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Alcaligenes sp. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.76 Å | ||||||
Authors | Wu, R. / Reger, A.S. / Cao, J. / Gulick, A.M. / Dunaway-Mariano, D. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: Rational redesign of the 4-chlorobenzoate binding site of 4-chlorobenzoate: coenzyme a ligase for expanded substrate range. Authors: Wu, R. / Reger, A.S. / Cao, J. / Gulick, A.M. / Dunaway-Mariano, D. | ||||||
History |
| ||||||
Remark 999 | SEQUENCE THE AUTHOR MENTIONED THAT THE SEQUENCE USED IN THIS ENTRY MATCHES THE GB ACCESSION CODE ...SEQUENCE THE AUTHOR MENTIONED THAT THE SEQUENCE USED IN THIS ENTRY MATCHES THE GB ACCESSION CODE AAN10109 AND IS MUTATED AT RESIDUE 303 (I303G). |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2qvy.cif.gz | 107.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2qvy.ent.gz | 81.5 KB | Display | PDB format |
PDBx/mmJSON format | 2qvy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2qvy_validation.pdf.gz | 443.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2qvy_full_validation.pdf.gz | 454.1 KB | Display | |
Data in XML | 2qvy_validation.xml.gz | 19.9 KB | Display | |
Data in CIF | 2qvy_validation.cif.gz | 27.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qv/2qvy ftp://data.pdbj.org/pub/pdb/validation_reports/qv/2qvy | HTTPS FTP |
-Related structure data
Related structure data | 2qvxC 2qvzC 2qw0C 1t5dS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 54325.004 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Alcaligenes sp. (bacteria) / Strain: AL3007 / Plasmid: pQE-70 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: Q8GN86*PLUS, EC: 6.2.1.33 |
---|---|
#2: Chemical | ChemComp-34Z / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 60.32 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.7 Details: 14-22% pentaerythritol propoxylate 426, 50 mM BTP, 1 mM ATP, 1 mM 3,4-DCB, pH 6.5-6.75, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 113 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F2 / Wavelength: 0.9793 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 31, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 2.76→30 Å / Num. obs: 17323 / % possible obs: 99.5 % / Redundancy: 5.2 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 11.5 |
Reflection shell | Resolution: 2.76→2.83 Å / Rmerge(I) obs: 0.525 / Mean I/σ(I) obs: 1.8 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1T5D Resolution: 2.76→30 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.914 / SU B: 30.392 / SU ML: 0.283 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.871 / ESU R Free: 0.344 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 57.054 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.76→30 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.76→2.833 Å / Total num. of bins used: 20
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group |
|