2H5Z
Crystallographic structure of digestive lysozyme 1 from Musca domestica bound to chitotetraose at 1.92 A resolution
Summary for 2H5Z
Entry DOI | 10.2210/pdb2h5z/pdb |
Related | 1HEW 2FBD |
Related PRD ID | PRD_900017 |
Descriptor | Lysozyme 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | lysozyme, ligant, musca domestica, hydrolase |
Biological source | Musca domestica (house fly) |
Total number of polymer chains | 2 |
Total formula weight | 28284.25 |
Authors | Valerio, A.A.,Cancado, F.C.,Marana, S.R.,Barbosa, J.A.R.G. (deposition date: 2006-05-29, release date: 2007-06-05, Last modification date: 2024-10-23) |
Primary citation | Marana, S.R.,Cancado, F.C.,Valerio, A.A.,Ferreira, C.,Terra, W.R.,Barbosa, J.A.R.G. Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica Acta Crystallogr.,Sect.F, 62:750-752, 2006 Cited by PubMed Abstract: Lysozymes are mostly known for their defensive role against bacteria, but in several animals lysozymes have a digestive function. Here, the initial crystallographic characterization of two digestive lysozymes from Musca domestica are presented. The proteins were crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data were collected to a maximum resolution of 1.9 angstroms using synchrotron radiation. The lysozyme 1 and 2 crystals belong to the monoclinic space group P2(1) (unit-cell parameters a = 36.52, b = 79.44, c = 45.20 angstroms, beta = 102.97 degrees) and the orthorhombic space group P2(1)2(1)2 (unit-cell parameters a = 73.90, b = 96.40, c = 33.27 angstroms), respectively. The crystal structures were solved by molecular replacement and structure refinement is in progress. PubMed: 16880547DOI: 10.1107/S1744309106024201 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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