1QQW

CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE

Summary for 1QQW

• Entry DOI: 10.2210/pdb1qqw/pdb
• Related: 4BLC
• Descriptor: CATALASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: heme protein, lattice contact, water, no nadp, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Peroxisome: P04040
• Total number of polymer chains: 4
• Total formula weight: 241813.93

Authors

Ko, T.P.,Safo, M.K.,Musayev, F.N.,Wang, C.,Wu, S.H.,Abraham, D.J. (deposition date: 1999-06-09, release date: 1999-06-14, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.75 Å)