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Yorodumi- PDB-1evq: THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 F... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1evq | ||||||
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Title | THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS | ||||||
Components | SERINE HYDROLASE | ||||||
Keywords | HYDROLASE / alpha/beta hydrolase fold | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Alicyclobacillus acidocaldarius (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | De Simone, G. / Galdiero, S. / Manco, G. / Lang, D. / Rossi, M. / Pedone, C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: A snapshot of a 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. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Crystallization and Preliminary X-ray Diffraction Studies of the Carboxylesterase EST2 from Alicyclobacillus acidocaldarius Authors: De Simone, G. / Manco, G. / Galdiero, S. / Lombardi, A. / Rossi, M. / Pavone, V. #2: Journal: Nat.Struct.Biol. / Year: 1999 Title: Crystal Structure of Brefeldin A Esterase, a Bacterial Homolog of the Mammalian Hormone-sensitive Lipase Authors: Wei, Y. / Contreras, J.A. / Sheffield, P. / Osterlund, T. / Derewenda, U. / Kneusel, R.E. / Matern, U. / Holm, C. / Derewenda, Z.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1evq.cif.gz | 65.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1evq.ent.gz | 53.4 KB | Display | PDB format |
PDBx/mmJSON format | 1evq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1evq_validation.pdf.gz | 452.8 KB | Display | wwPDB validaton report |
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Full document | 1evq_full_validation.pdf.gz | 460.7 KB | Display | |
Data in XML | 1evq_validation.xml.gz | 15.6 KB | Display | |
Data in CIF | 1evq_validation.cif.gz | 21 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ev/1evq ftp://data.pdbj.org/pub/pdb/validation_reports/ev/1evq | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a monomer |
-Components
#1: Protein | Mass: 34526.551 Da / Num. of mol.: 1 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, carboxylesterase |
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#2: Chemical | ChemComp-EPE / |
#3: Chemical | ChemComp-TRS / |
#4: 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: 2.43 Å3/Da / Density % sol: 48.8 % Description: Wavelength 0.9785 is the peak wavelength, 0.9786 is the inflection, and 0.9810 is remote. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: 2% PEG 400, 100mM Hepes pH 7.8, 2M Ammonium Sulphate, 1mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 22K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: X31 / Wavelength: 0.9785, 0.9786, 0.9810 | ||||||||||||
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Mar 10, 1999 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.6→100 Å / Num. all: 203297 / Num. obs: 10886 / % possible obs: 99.4 % / Redundancy: 18 % / Rmerge(I) obs: 0.058 / Net I/σ(I): 31 | ||||||||||||
Reflection shell | Resolution: 2.6→2.69 Å / Rmerge(I) obs: 0.236 / Num. unique all: 1057 / % possible all: 100 | ||||||||||||
Reflection shell | *PLUS % possible obs: 100 % / Mean I/σ(I) obs: 8.8 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.6→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.216 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.6 |