+Open data
-Basic information
Entry | Database: PDB / ID: 1jpo | ||||||
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Title | LOW TEMPERATURE ORTHORHOMBIC LYSOZYME | ||||||
Components | LYSOZYME | ||||||
Keywords | HYDROLASE / GLYCOSIDASE | ||||||
Function / homology | Function and homology information Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium ...Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Bradbrook, G.M. / Helliwell, J.R. / Habash, J. | ||||||
Citation | Journal: Time-Resolved Electron and X-Ray Diffraction; 13-14 July 1995, San Diego, California (in: Proc.Spie-Int.Soc.Opt.Eng., V.2521) Year: 1995 Title: Time-Resolved Biological and Perturbation Chemical Crystallography: Laue and Monochromatic Developments Authors: Bradbrook, S. / Deacon, A. / Habash, J. / Helliwell, J.R. / Helliwell, M. / Nieh, Y.P. / Snell, E.H. / Trapani, G. / Thompson, A.W. / Campbell, J.W. / Allinson, N.M. / Moon, K. / Ursby, T. / Wulff, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jpo.cif.gz | 32.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jpo.ent.gz | 25.4 KB | Display | PDB format |
PDBx/mmJSON format | 1jpo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jp/1jpo ftp://data.pdbj.org/pub/pdb/validation_reports/jp/1jpo | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14331.160 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / Cell: EGG / Cellular location: CYTOPLASM (WHITE) / References: UniProt: P00698, lysozyme |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 45 % |
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 0.7 / Wavelength: 0.7, 1.7 | |||||||||
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE AREA DETECTOR | |||||||||
Radiation | Monochromatic (M) / Laue (L): L / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Num. obs: 6424 / % possible obs: 87.3 % / Rmerge(I) obs: 0.121 |
-Processing
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Refinement | Highest resolution: 2.1 Å /
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Refinement step | Cycle: LAST / Highest resolution: 2.1 Å
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Refine LS restraints |
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