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Open data
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Basic information
Entry | Database: PDB / ID: 1u4n | ||||||
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Title | Crystal Structure Analysis of the M211S/R215L EST2 mutant | ||||||
![]() | CARBOXYLESTERASE EST2 | ||||||
![]() | HYDROLASE / ALPHA/BETA HYDROLASE FOLD | ||||||
Function / homology | short-chain carboxylesterase activity / Alpha/beta hydrolase fold-3 / alpha/beta hydrolase fold / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / Hydrolase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | De Simone, G. / Menchise, V. / Alterio, V. / Mandrich, L. / Rossi, M. / Manco, G. / Pedone, C. | ||||||
![]() | ![]() Title: The Crystal Structure of an EST2 Mutant Unveils Structural Insights on the H Group of the Carboxylesterase/Lipase Family. Authors: De Simone, G. / Menchise, V. / Alterio, V. / Mandrich, L. / Rossi, M. / Manco, G. / Pedone, C. #1: ![]() 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. #2: ![]() 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.2 KB | Display | ![]() |
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PDB format | ![]() | 57.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.8 KB | Display | ![]() |
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Full document | ![]() | 437.4 KB | Display | |
Data in XML | ![]() | 15.7 KB | Display | |
Data in CIF | ![]() | 23 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1evqS S: Starting model for refinement |
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Similar structure data |
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Links
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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: 34250.820 Da / Num. of mol.: 1 / Mutation: M211S, R215L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Plasmid: PT7-7SCII / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 39.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 8000, Tris/HCl, 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: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 25, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 17360 / % possible obs: 89.5 % / Observed criterion σ(I): -3 / Rsym value: 0.068 / Net I/σ(I): 20.7 |
Reflection shell | Resolution: 2.1→2.14 Å / Mean I/σ(I) obs: 6.5 / Rsym value: 0.208 / % possible all: 87.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EVQ Resolution: 2.1→20 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.1→2.15 Å /
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