1aln
From Proteopedia
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CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE COMPLEXED WITH 3-DEAZACYTIDINE
Overview
The cytidine deaminase substrate analog inhibitor 3-deazacytidine binds, with its 4-amino group inserted into a site previously identified as a, probable binding site for the leaving ammonia group. Binding to this site, shifts the pyrimidine ring significantly further from the activated water, molecule than the position it occupies in either of two complexes with, compounds capable of hydrogen bonding at the 3-position of the ring [Xiang, et al. (1995) Biochemistry 34, 4516-4523]. Difference Fourier maps between, the deazacytidine, dihydrozebularine, and zebularine--hydrate inhibitor, complexes suggest that the ring itself moves successively toward the, activated water, leaving the amino group behind in this site as the, substrate complex approaches the transition state. They also reveal, ... [(full description)]
About this Structure
1ALN is a [Single protein] structure of sequence from [Escherichia coli] with ZN and CTD as [ligands]. Active as [Cytidine deaminase], with EC number [3.5.4.5]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
Reference
Cytidine deaminase complexed to 3-deazacytidine: a "valence buffer" in zinc enzyme catalysis., Xiang S, Short SA, Wolfenden R, Carter CW Jr, Biochemistry. 1996 Feb 6;35(5):1335-41. PMID:8634261
Page seeded by OCA on Tue Oct 30 14:49:37 2007
Categories: Cytidine deaminase | Escherichia coli | Single protein | Carter, C.W. | Xiang, S. | CTD | ZN | Hydrolase | Substrate | Valence buffer | Zinc enzyme
