1SFB
BINDING OF PENTA-N-ACETYLCHITOPENTAOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY
Summary for 1SFB
| Entry DOI | 10.2210/pdb1sfb/pdb |
| Related | 1JA7 1SF4 1SF6 1SF7 1SFG |
| Descriptor | LYSOZYME, 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-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | powder diffraction; rietveld refinement; lysozyme, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 15365.14 |
| Authors | Von Dreele, R.B. (deposition date: 2004-02-19, release date: 2004-03-02, Last modification date: 2024-10-16) |
| Primary citation | Von Dreele, R.B. Binding of N-acetylglucosamine oligosaccharides to hen egg-white lysozyme: a powder diffraction study. Acta Crystallogr.,Sect.D, 61:22-32, 2005 Cited by PubMed Abstract: The binding of N-acetylglucosamine oligosaccharides (NAGn, n = 2-6) to hen egg-white lysozyme (HEWL; EC 3.2.1.17) was investigated by X-ray powder diffraction at room temperature. Each NAGn examined was found to bind to lysozyme in rapid-precipitation preparations in 1.0 M NaCl pH 6.0 buffer. The location of each NAGn was easily found from difference Fourier maps generated from structure factors extracted during preliminary Rietveld refinements. Full NAGn-protein structures were subjected to combined Rietveld and stereochemical restraint refinements (Rwp = 2.28-2.59%; Rp = 1.81-2.04%; RF2 = 3.91-5.80%) and revealed binding modes for NAGn that depended on the length of the NAG oligosaccharide. The NAG2 ligand was found in the BC sites in the cleft of HEWL, NAG3 was found to bind in both the ABC and BCD sites in the ratio 35:65 and NAG4 and NAG5 bound to the ABCD and ABCDE sites, respectively, while NAG6 only bound to sites ABCDE, leaving the F site empty with the remaining saccharide ring located in a solvent region adjacent to the A site. All protein powder diffraction patterns in this study consisted of extremely sharp Bragg peaks consistent with approximately 1 microm crystallites that were devoid of line-broadening defects. Details of the stereochemical restraints used in these refinements and their impact on structural validation are also discussed. PubMed: 15608372DOI: 10.1107/S0907444904025715 PDB entries with the same primary citation |
| Experimental method | POWDER DIFFRACTION |
Structure validation
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