+Open data
-Basic information
Entry | Database: PDB / ID: 2hm7 | ||||||
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Title | Crystal Structure Analysis of the G84S EST2 mutant | ||||||
Components | Carboxylesterase | ||||||
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 Å | ||||||
Authors | Menchise, V. / Alterio, V. / De Simone, G. | ||||||
Citation | Journal: Proteins / Year: 2007 Title: Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius. Authors: Mandrich, L. / Menchise, V. / Alterio, V. / De Simone, G. / Pedone, C. / Rossi, M. / 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 | 2hm7.cif.gz | 77.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hm7.ent.gz | 56.3 KB | Display | PDB format |
PDBx/mmJSON format | 2hm7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hm7_validation.pdf.gz | 433.3 KB | Display | wwPDB validaton report |
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Full document | 2hm7_full_validation.pdf.gz | 436.9 KB | Display | |
Data in XML | 2hm7_validation.xml.gz | 14.9 KB | Display | |
Data in CIF | 2hm7_validation.cif.gz | 20.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hm/2hm7 ftp://data.pdbj.org/pub/pdb/validation_reports/hm/2hm7 | 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 34368.996 Da / Num. of mol.: 1 / Mutation: G84S 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-SO4 / |
#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: 1.82 Å3/Da / Density % sol: 32.54 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 18% PEG 8000, 0.1M TRIS/HCl, 0.2M MAGNESIUM CHLORIDE, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. all: 17662 / Num. obs: 17662 / % possible obs: 97.8 % / Rsym value: 0.056 / Net I/σ(I): 17.7 |
Reflection shell | Highest resolution: 2 Å / Mean I/σ(I) obs: 6.8 / Rsym value: 0.137 / % possible all: 80.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EVQ Resolution: 2→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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