1BCD

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

1BCD の概要

• エントリーDOI: 10.2210/pdb1bcd/pdb
• 分子名称: CARBONIC ANHYDRASE II, ZINC ION, TRIFLUOROMETHANE SULFONAMIDE, ... (4 entities in total)
• 機能のキーワード: lyase(oxo-acid)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : P00918
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29372.36

構造登録者

Hakansson, K.,Liljas, A. (登録日: 1993-08-31, 公開日: 1993-10-31, 最終更新日: 2024-02-07)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.9 Å)