The structure of human carbonic anhydrase II in complex with bromide and azide.
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.
Jönsson
B M
BM
Department of Biophysics, Lund University, Sweden.
Håkansson
K
K
Liljas
A
A
D001386:Azides; D001665:Binding Sites; D001965:Bromides; D002256:Carbonic Anhydrases / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction
D001386:Azides; D001965:Bromides; D002256:Carbonic Anhydrases