+Open data
-Basic information
Entry | Database: PDB / ID: 2yh2 | ||||||
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Title | Pyrobaculum calidifontis esterase monoclinic form | ||||||
Components | ESTERASE | ||||||
Keywords | HYDROLASE / HYPERTHERMOPHILIC ENZYME / TERTIARY ALCOHOL / ALPHA/BETA HYDROLASE FOLD | ||||||
Function / homology | Function and homology information | ||||||
Biological species | PYROBACULUM CALIDIFONTIS (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Palm, G.J. / Bogdanovic, X. / Hinrichs, W. | ||||||
Citation | Journal: Appl.Microbiol.Biotechnol. / Year: 2011 Title: The Crystal Structure of an Esterase Fom the Hyperthermophilic Microorganism Pyrobaculum Calidifontis Va1 Supports Explanation of its Enantioselectivity. Authors: Palm, G.J. / Fernandez-Alvaro, E. / Bogdanovic, X. / Bartsch, S. / Sczodrok, J. / Singh, R.K. / Boettcher, D. / Atomi, H. / Bornscheuer, U.T. / Hinrichs, W. #1: Journal: Appl.Environ.Microbiol. / Year: 2002 Title: Extremely Stable and Versatile Carboxylesterase from a Hyperthermophilic Archaeon. Authors: Hotta, Y. / Ezaki, S. / Atomi, H. / Imanaka, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2yh2.cif.gz | 476.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2yh2.ent.gz | 395.3 KB | Display | PDB format |
PDBx/mmJSON format | 2yh2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yh/2yh2 ftp://data.pdbj.org/pub/pdb/validation_reports/yh/2yh2 | HTTPS FTP |
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-Related structure data
Related structure data | 3zwqC 2wir C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 34396.266 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) PYROBACULUM CALIDIFONTIS (archaea) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q8NKS0, carboxylesterase #2: Chemical | ChemComp-SO4 / | #3: 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: 2.14 Å3/Da / Density % sol: 43 % / Description: NONE |
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Crystal grow | pH: 8 Details: 10% PEG 4000, 30% MPD, 0.1 M IMIDAZOLE PH 8.0; SOAKED IN 10% PEG 4000, 4% DMSO, 0.1 M IMIDAZOLE PH 8.0, 0.01 M PHENYLBUTANOIC ACID ETHYL ESTER. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 0.97784 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 1, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97784 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→10 Å / Num. obs: 50355 / % possible obs: 85 % / Observed criterion σ(I): -3 / Redundancy: 5 % / Biso Wilson estimate: 17.6 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 5.3 |
Reflection shell | Resolution: 2.2→2.25 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 3.5 / % possible all: 47 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2WIR 2wir Resolution: 2.2→141.87 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.915 / SU B: 11.584 / SU ML: 0.135 / Cross valid method: THROUGHOUT / ESU R: 0.435 / ESU R Free: 0.231 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.688 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→141.87 Å
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Refine LS restraints |
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