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- PDB-1ov7: T4 Lysozyme Cavity Mutant L99A/M102Q Bound with 2-Allyl-6-Methyl-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ov7 | ||||||
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Title | T4 Lysozyme Cavity Mutant L99A/M102Q Bound with 2-Allyl-6-Methyl-Phenol | ||||||
![]() | Lysozyme | ||||||
![]() | HYDROLASE / GLYCOSIDASE / BACTERIOLYTIC ENZYME | ||||||
Function / homology | ![]() viral release from host cell by cytolysis / peptidoglycan catabolic process / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / host cell cytoplasm / defense response to bacterium Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wei, B.Q. / Baase, W.A. / Weaver, L.H. / Matthews, B.W. / Shoichet, B.K. | ||||||
![]() | ![]() Title: Testing a Flexible-receptor Docking Algorithm in a Model Binding Site Authors: Wei, B.Q. / Weaver, L.H. / Ferrari, A.M. / Matthews, B.W. / Shoichet, B.K. #1: ![]() Title: A Model Binding Site for Testing Scoring Functions in Molecular Docking Authors: Wei, B.Q. / Baase, W.A. / Weaver, L.H. / Matthews, B.W. / Shoichet, B.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 47.4 KB | Display | ![]() |
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PDB format | ![]() | 32.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.7 KB | Display | ![]() |
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Full document | ![]() | 451.2 KB | Display | |
Data in XML | ![]() | 9.9 KB | Display | |
Data in CIF | ![]() | 12.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ov5C ![]() 1ovhC ![]() 1ovjC ![]() 1ovkC ![]() 1owyC ![]() 1owzC ![]() 1lguS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 18617.320 Da / Num. of mol.: 1 / Mutation: L99A, M102Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-LYL / | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.22 % |
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: UCSD MARK II / Detector: AREA DETECTOR |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→13 Å / Num. all: 15008 / Num. obs: 15008 / % possible obs: 89 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.081 / Net I/σ(I): 10 |
Reflection shell | Resolution: 1.9→2 Å / Rmerge(I) obs: 0.16 / Mean I/σ(I) obs: 2.1 / Num. unique all: 2206 / % possible all: 67 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1LGU Resolution: 2→13 Å / Isotropic thermal model: isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→13 Å
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Refine LS restraints |
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