1BCD

X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE

Summary for 1BCD

Entry DOI	10.2210/pdb1bcd/pdb
Descriptor	CARBONIC ANHYDRASE II, ZINC ION, TRIFLUOROMETHANE SULFONAMIDE, ... (4 entities in total)
Functional Keywords	lyase(oxo-acid)
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm : P00918
Total number of polymer chains	1
Total formula weight	29372.36
Authors	Hakansson, K.,Liljas, A. (deposition date: 1993-08-31, release date: 1993-10-31, Last modification date: 2024-02-07)
Primary citation	Hakansson, K.,Liljas, A. The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide. FEBS Lett., 350:319-322, 1994 Cited by PubMed Abstract: It has recently been shown that aliphatic sulphonamides are good inhibitors of carbonic anhydrase (CA) provided that the pK of the sulphonamide is low. We have determined the structure of the complex between CAII and CF3SO2NH2 by X-ray crystallographic methods. The nitrogen of the sulphonamide is bound to the zinc ion of the enzyme in the usual manner. The other parts of the inhibitor show a different mode of binding from aromatic sulphonamides since the trifluoromethyl group is bound at the hydrophobic part of the active site instead of pointing out from the active site. It should be possible to design new inhibitors specific for the different isoenzymes, starting from the present structure. PubMed: 8070585 DOI: 10.1016/0014-5793(94)00798-5 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation