Summary for 135L
| Entry DOI | 10.2210/pdb135l/pdb |
| Descriptor | TURKEY EGG WHITE LYSOZYME (2 entities in total) |
| Functional Keywords | hydrolase(o-glycosyl) |
| Biological source | Meleagris gallopavo (turkey) |
| Cellular location | Secreted: P00703 |
| Total number of polymer chains | 1 |
| Total formula weight | 14228.10 |
| Authors | Harata, K. (deposition date: 1993-06-10, release date: 1993-10-31, Last modification date: 2024-10-30) |
| Primary citation | Harata, K. X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution. Acta Crystallogr.,Sect.D, 49:497-504, 1993 Cited by PubMed Abstract: Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties. PubMed: 15299509DOI: 10.1107/S0907444993005542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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