1aqp
From Proteopedia
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RIBONUCLEASE A COPPER COMPLEX
Overview
We report the crystal structures of the copper and nickel complexes of, RNase A. The overall topology of these two complexes is similar to that of, other RNase A structures. However, there are significant differences in, the mode of binding of copper and nickel. There are two copper ions per, molecule of the protein, but there is only one nickel ion per molecule of, the protein. Significant changes occur in the interprotein interactions as, a result of differences in the coordinating groups at the common binding, site around His-105. Consequently, the copper- and nickel-ion-bound dimers, of RNase A act as nucleation sites for generating different crystal, lattices for the two complexes. A second copper ion is present at an, active site residue His-119 for which all the ligands are from ... [(full description)]
About this Structure
1AQP is a [Single protein] structure of sequence from [Bos taurus] with CU as [ligand]. Active as [[1]], with EC number [3.1.27.5]. Full crystallographic information is available from [OCA].
Reference
Crystal structures of the copper and nickel complexes of RNase A: metal-induced interprotein interactions and identification of a novel copper binding motif., Balakrishnan R, Ramasubbu N, Varughese KI, Parthasarathy R, Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9620-5. PMID:9275172
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