Jönsson B M, Håkansson K, Liljas A
Department of Biophysics, Lund University, Sweden.
FEBS Lett. 1993 May 10;322(2):186-90. doi: 10.1016/0014-5793(93)81565-h.
The three-dimensional structure of human carbonic anhydrase II complexed with azide and with bromide was investigated crystallographically. Both of these non-protonated inhibitors replace the zinc and the 'deep' water, two catalytically important water molecules in the active site of the molecule. Both the azide and the bromide ions bind in a distorted tetrahedral manner 0.4 and 1.1 A from the zinc water position, respectively, but are in close contact (2.0 and 2.6 A, respectively) with the zinc ion.
通过晶体学研究了与叠氮化物和溴化物复合的人碳酸酐酶II的三维结构。这两种非质子化抑制剂都取代了锌和“深层”水,这是该分子活性位点中两个对催化至关重要的水分子。叠氮离子和溴离子均以扭曲的四面体方式结合,分别距锌水位置0.4埃和1.1埃,但与锌离子紧密接触(分别为2.0埃和2.6埃)。