1AT6
HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
Summary for 1AT6
| Entry DOI | 10.2210/pdb1at6/pdb |
| Related PRD ID | PRD_900017 |
| 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 (3 entities in total) |
| Functional Keywords | isoaspartate, hydrolase, o-glycosyl hydrolase |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Secreted: P00698 |
| Total number of polymer chains | 1 |
| Total formula weight | 14958.75 |
| Authors | Noguchi, S.,Miyawaki, K.,Satow, Y. (deposition date: 1997-08-19, release date: 1998-02-25, Last modification date: 2024-11-20) |
| Primary citation | Noguchi, S.,Miyawaki, K.,Satow, Y. Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose. J.Mol.Biol., 278:231-238, 1998 Cited by PubMed Abstract: The isomerization of Asp101 to isoaspartate autocatalytically proceeds via a succinimide intermediate in hen egg-white lysozyme at a mildly acidic condition. The crystal structures of succinimide and isoaspartate forms of the lysozyme proteins, each complexed with a tri-N-acetylchitotriose ligand, have been determined at 1.8 A resolution, and distinctively elucidate coplanar cyclic aminosuccinyl and beta-linked isoaspartyl residues. Compared with the liganded native protein with normal Asp101, succinimide 101 protrudes toward the ligand, and isoaspartate 101 extends away from the ligand. The formations of these residues caused the loss of three hydrogen-bonds between the ligand and the side-chains of Asp101 and Asn103 along with 0.5 A displacement of the ligand location. PubMed: 9571046DOI: 10.1006/jmbi.1998.1674 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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