1BIC

CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-

1BIC の概要

• エントリーDOI: 10.2210/pdb1bic/pdb
• 分子名称: CARBONIC ANHYDRASE II, ZINC ION, BICARBONATE ION, ... (5 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: 29536.96

構造登録者

Xue, Y.,Vidgren, J.,Svensson, L.A.,Liljas, A.,Jonsson, B.-H.,Lindskog, S. (登録日: 1992-09-01, 公開日: 1993-10-31, 最終更新日: 2024-02-07)

主引用文献

Xue, Y.,Vidgren, J.,Svensson, L.A.,Liljas, A.,Jonsson, B.H.,Lindskog, S.
Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-.
Proteins, 15:80-87, 1993

PubMed Abstract: A complex of carbonic anhydrase (CA) with one of its substrates, bicarbonate, has been studied crystallographically. Human isoenzyme II was mutated at position 200 from threonine to histidine, which results in higher affinity for bicarbonate. The HCO3- ion binds in the active site to the zinc ion as a pseudo-bidentate ligand which gives the metal a coordination geometry between tetrahedral and trigonal bipyramide. The water/hydroxide normally bound with tetrahedral coordination to the zinc is probably replaced by the OH group of the bicarbonate ion. The importance of residues Thr-199 and Glu-106 in controlling the binding orientation of HCO3- is discussed as well as the catalytic mechanism. Both the complex as well as the uncomplexed mutant were studied at 1.9 A resolution.

PubMed: 8451242
DOI: 10.1002/prot.340150110

実験手法

X-RAY DIFFRACTION (1.9 Å)