3FFP

X ray structure of the complex between carbonic anhydrase II and LC inhibitors

3FFP の概要

• エントリーDOI: 10.2210/pdb3ffp/pdb
• 分子名称: Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (6 entities in total)
• 機能のキーワード: carbonic anhydrase, inhibitors, acetylation, cytoplasm, disease mutation, lyase, metal-binding, polymorphism, zinc
• 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: 29957.51

構造登録者

Temperini, C.,Crocetti, L.,Scozzafava, A.,Supuran, C.T. (登録日: 2008-12-04, 公開日: 2009-08-18, 最終更新日: 2023-11-01)

主引用文献

Crocetti, L.,Maresca, A.,Temperini, C.,Hall, R.A.,Scozzafava, A.,Muhlschlegel, F.A.,Supuran, C.T.
A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases
Bioorg.Med.Chem.Lett., 19:1371-1375, 2009

PubMed Abstract: A sulfonamide derivative of the antihelmintic drug thiabendazole was prepared and investigated for inhibition of the zinc enzyme carbonic anhydrase CA (EC 4.2.1.1). Mammalian isoforms CA I-XIV and the nematode enzyme of Caenorhabditis elegans CAH-4b were included in this study. Thiabendazole-5-sulfonamide was a very effective inhibitor of CAH-4b and CA IX (K(I)s of 6.4-9.5nm) and also inhibited effectively isozymes CA I, II, IV-VII, and XII, with K(I)s in the range of 17.8-73.2nM. The high resolution X-ray crystal structure of its adduct with isozyme II evidenced the structural elements responsible for this potent inhibitory activity.

PubMed: 19186056
DOI: 10.1016/j.bmcl.2009.01.038

実験手法

X-RAY DIFFRACTION (1.81 Å)