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Yorodumi- PDB-185l: SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 185l | ||||||
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Title | SPECIFICITY OF LIGAND BINDING IN A BURIED NON-POLAR CAVITY OF T4 LYSOZYME: LINKAGE OF DYNAMICS AND STRUCTURAL PLASTICITY | ||||||
Components | T4 LYSOZYME | ||||||
Keywords | HYDROLASE (O-GLYCOSYL) | ||||||
Function / homology | Function and homology information 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 | Enterobacteria phage T4 (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Morton, A. / Matthews, B.W. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity. Authors: Morton, A. / Matthews, B.W. #1: Journal: To be Published Title: Energetic Origins of Specificity of Ligand Binding in an Interior Cavity of T4 Lysozyme Authors: Morton, A. / Baase, W.A. / Matthews, B.W. #2: Journal: J.Mol.Biol. / Year: 1987 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 185l.cif.gz | 47.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb185l.ent.gz | 33.4 KB | Display | PDB format |
PDBx/mmJSON format | 185l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 185l_validation.pdf.gz | 419.1 KB | Display | wwPDB validaton report |
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Full document | 185l_full_validation.pdf.gz | 421.4 KB | Display | |
Data in XML | 185l_validation.xml.gz | 6.2 KB | Display | |
Data in CIF | 185l_validation.cif.gz | 8.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/85/185l ftp://data.pdbj.org/pub/pdb/validation_reports/85/185l | HTTPS FTP |
-Related structure data
Related structure data | 181lC 182lC 183lC 184lC 186lC 187lC 188lC 1nhbC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18586.283 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage T4 (virus) / Genus: T4-like viruses / Species: Enterobacteria phage T4 sensu lato / Plasmid: M13 / References: UniProt: P00720, lysozyme | ||||||
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#2: Chemical | #3: Chemical | ChemComp-HED / | #4: Chemical | ChemComp-IND / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.95 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 7.1 / PH range high: 6.3 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 20 Å / Num. obs: 41721 / % possible obs: 79 % / Observed criterion σ(I): 0 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.8→20 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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