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Yorodumi- PDB-1qz3: CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qz3 | ||||||
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Title | CRYSTAL STRUCTURE OF MUTANT M211S/R215L OF CARBOXYLESTERASE EST2 COMPLEXED WITH HEXADECANESULFONATE | ||||||
Components | CARBOXYLESTERASE EST2 | ||||||
Keywords | HYDROLASE / ALPHA/BETA HYDROLASE FOLD | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Alicyclobacillus acidocaldarius (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | De Simone, G. / Mandrich, L. / Menchise, V. / Giordano, V. / Febbraio, F. / Rossi, M. / Pedone, C. / Manco, G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis. Authors: De Simone, G. / Mandrich, L. / Menchise, V. / Giordano, V. / Febbraio, F. / Rossi, M. / Pedone, C. / Manco, G. #1: Journal: J.Mol.Biol. / Year: 2000 Title: A SNAPSHOT OF THE TRANSITION STATE ANALOGUE OF A NOVEL THERMOPHILIC ESTERASE BELONGING TO THE SUBFAMILY OF MAMMALIAN HORMONE-SENSITIVE LIPASE Authors: DE SIMONE, G. / GALDIERO, S. / MANCO, G. / LANG, D. / ROSSI, M. / PEDONE, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qz3.cif.gz | 79.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qz3.ent.gz | 58.8 KB | Display | PDB format |
PDBx/mmJSON format | 1qz3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qz3_validation.pdf.gz | 612.5 KB | Display | wwPDB validaton report |
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Full document | 1qz3_full_validation.pdf.gz | 616.2 KB | Display | |
Data in XML | 1qz3_validation.xml.gz | 16.4 KB | Display | |
Data in CIF | 1qz3_validation.cif.gz | 24 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qz/1qz3 ftp://data.pdbj.org/pub/pdb/validation_reports/qz/1qz3 | HTTPS FTP |
-Related structure data
Related structure data | 1evqS 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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-Components
#1: Protein | Mass: 34250.820 Da / Num. of mol.: 1 / Mutation: R215L, M211S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Alicyclobacillus acidocaldarius (bacteria) Plasmid: PT7-7SCII / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q7SIG1 |
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#2: Chemical | ChemComp-HDS / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.74 Å3/Da / Density % sol: 55.13 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: AMMONIUM SULPHATE, TRIS BUFFER, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X13 / Wavelength: 0.8015 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8015 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. obs: 17707 / % possible obs: 98.8 % / Rsym value: 0.089 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 2.3→2.34 Å / Mean I/σ(I) obs: 2.2 / Rsym value: 0.426 / % possible all: 94.1 |
Reflection | *PLUS Num. measured all: 177515 / Rmerge(I) obs: 0.089 |
Reflection shell | *PLUS % possible obs: 94.1 % / Rmerge(I) obs: 0.426 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EVQ Resolution: 2.3→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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Xplor file |
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Refinement | *PLUS % reflection Rfree: 5 % | ||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||
Displacement parameters | *PLUS |