4Q6D

Crystal structure of human carbonic anhydrase isozyme II with 4-[(Z)-azepan-1-yldiazenyl]benzenesulfonamide

4Q6D の概要

• エントリーDOI: 10.2210/pdb4q6d/pdb
• 関連するPDBエントリー: 4Q6E
• 分子名称: Carbonic anhydrase 2, ZINC ION, DIMETHYL SULFOXIDE, ... (6 entities in total)
• 機能のキーワード: drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• 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: 29878.14

構造登録者

Smirnov, A.,Manakova, E.,Grazulis, S. (登録日: 2014-04-22, 公開日: 2014-11-26, 最終更新日: 2023-09-20)

主引用文献

Rutkauskas, K.,Zubriene, A.,Tumosiene, I.,Kantminiene, K.,Kazemekaite, M.,Smirnov, A.,Kazokaite, J.,Morkunaite, V.,Capkauskaite, E.,Manakova, E.,Grazulis, S.,Beresnevicius, Z.J.,Matulis, D.
4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.
Molecules, 19:17356-17380, 2014

PubMed Abstract: A series of N-aryl-β-alanine derivatives and diazobenzenesulfonamides containing aliphatic rings were designed, synthesized, and their binding to carbonic anhydrases (CA) I, II, VI, VII, XII, and XIII was studied by the fluorescent thermal shift assay and isothermal titration calorimetry. The results showed that 4-substituted diazobenzenesulfonamides were more potent CA binders than N-aryl-β-alanine derivatives. Most of the N-aryl-β-alanine derivatives showed better affinity for CA II while diazobenzenesulfonamides possessed nanomolar affinities towards CA I isozyme. X-ray crystallographic structures showed the modes of binding of both compound groups.

PubMed: 25353386
DOI: 10.3390/molecules191117356

実験手法

X-RAY DIFFRACTION (1.12 Å)