1at5 | pdb_00001at5
HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE
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| 1at5, resolution 1.80Å | |||||||||||||
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| Sites: | SUC | ||||||||||||
| Ligands: | NA and CL | ||||||||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1AT5 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose., Noguchi S, Miyawaki K, Satow Y, J Mol Biol. 1998 Apr 24;278(1):231-8. PMID:9571046
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