1c5h
From Proteopedia
HYDROGEN BONDING AND CATALYSIS: AN UNEXPECTED EXPLANATION FOR HOW A SINGLE AMINO ACID SUBSTITUTION CAN CHANGE THE PH OPTIMUM OF A GLYCOSIDASE
Template:ABSTRACT PUBMED 10860737
About this Structure
1C5H is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.
Reference
Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase., Joshi MD, Sidhu G, Pot I, Brayer GD, Withers SG, McIntosh LP, J Mol Biol. 2000 May 26;299(1):255-79. PMID:10860737
Page seeded by OCA on Mon Jun 30 20:14:09 2008
Categories: Bacillus circulans | Endo-1,4-beta-xylanase | Single protein | Brayer, G D. | Joshi, M D. | Mcintosh, L P. | Pot, I. | Sidhu, G. | Withers, S G. | General acid/ base catalysis | Glycosidase | Isotope shift | Nmr | Ph-dependent enzyme mechanism | Short hydrogen bond | X-ray cyrstallography | Xylan