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- PDB-152l: CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 L... -
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Open data
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Basic information
Entry | Database: PDB / ID: 152l | ||||||
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Title | CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME | ||||||
![]() | T4 LYSOZYME | ||||||
![]() | HYDROLASE(O-GLYCOSYL) | ||||||
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 | ![]() | ||||||
![]() | Matsumura, M. / Weaver, L.H. / Matthews, B.W. | ||||||
![]() | ![]() Title: Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme. Authors: Zhang, X.J. / Matthews, B.W. #1: ![]() Title: A Covalent Enzyme-Substrate Intermediate with Saccharide Distorsion in a Mutant T4 Lysozyme Authors: Kuroki, R. / Weaver, L.H. / Matthews, B.W. #2: ![]() Title: Structure of a Stabilizing Disulfide Bridge Mutant that Closes the Active-Site Cleft of T4 Lysozyme Authors: Jacobson, R.H. / Matsumura, M. / Faber, H.R. / Matthews, B.W. #3: ![]() Title: Structure of a Thermostable Disulfide-Bridge Mutant of Phage T4 Lysozyme Shows that an Engineered Cross-Link in a Flexible Region Does not Increase the Rigidity of the Folded Protein Authors: Pjura, P.E. / Matsumura, M. / Wozniak, J.A. / Matthews, B.W. #4: ![]() Title: Substantial Increase of Protein Stability by Multiple Disulphide Bonds Authors: Matsumura, M. / Signor, G. / Matthews, B.W. #5: ![]() Title: Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution Authors: Weaver, L.H. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 42.3 KB | Display | ![]() |
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PDB format | ![]() | 32.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.8 KB | Display | ![]() |
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Full document | ![]() | 438.5 KB | Display | |
Data in XML | ![]() | 9.2 KB | Display | |
Data in CIF | ![]() | 11.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 18634.461 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
Sequence details | SEQUENCE ADVISORY NOTICE DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE DIFFERENCE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.08 Å3/Da / Density % sol: 40.98 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Ambient pressure: 101 kPa / Mean temperature: 298 K |
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Diffraction source | Source: rotating-anode X-ray tube / Type: RIGAKU RU200 / Target: Cu |
Detector | Type: AREA DETECTOR / Detector: AREA DETECTOR / Details: Xuong-Hamlin |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray / Wavelength: 1.5418 Å |
Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Resolution: 2→50 Å / Rfactor obs: 0.168 / σ(F): 0 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 50 Å / σ(F): 0 / Rfactor all: 0.168 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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