1at6: Difference between revisions
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|PDB= 1at6 |SIZE=350|CAPTION= <scene name='initialview01'>1at6</scene>, resolution 1.80Å | |PDB= 1at6 |SIZE=350|CAPTION= <scene name='initialview01'>1at6</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=IAS:ASP+101+Isomerized+To+Isoaspartate'>IAS</scene> | |SITE= <scene name='pdbsite=IAS:ASP+101+Isomerized+To+Isoaspartate'>IAS</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=IAS:ASPARTYL+GROUP'>IAS</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1at6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1at6 OCA], [http://www.ebi.ac.uk/pdbsum/1at6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1at6 RCSB]</span> | |||
}} | }} | ||
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[[Category: o-glycosyl hydrolase]] | [[Category: o-glycosyl hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:01 2008'' | ||
Revision as of 18:47, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
OverviewOverview
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 StructureAbout this Structure
1AT6 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
ReferenceReference
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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