1QQW

CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE

1QQW の概要

• エントリーDOI: 10.2210/pdb1qqw/pdb
• 関連するPDBエントリー: 4BLC
• 分子名称: CATALASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: heme protein, lattice contact, water, no nadp, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Peroxisome: P04040
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 241813.93

構造登録者

Ko, T.P.,Safo, M.K.,Musayev, F.N.,Wang, C.,Wu, S.H.,Abraham, D.J. (登録日: 1999-06-09, 公開日: 1999-06-14, 最終更新日: 2024-02-14)

主引用文献

Ko, T.P.,Safo, M.K.,Musayev, F.N.,Di Salvo, M.L.,Wang, C.,Wu, S.H.,Abraham, D.J.
Structure of human erythrocyte catalase.
Acta Crystallogr.,Sect.D, 56:241-245, 2000

PubMed Abstract: Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.

PubMed: 10666617
DOI: 10.1107/S0907444999015930

実験手法

X-RAY DIFFRACTION (2.75 Å)