1F4J
STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE
Summary for 1F4J
Entry DOI | 10.2210/pdb1f4j/pdb |
Related | 1qqw |
Descriptor | CATALASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | heme protein, no bound nadph, oxidoreductase |
Biological source | Homo sapiens (human) |
Cellular location | Peroxisome: P04040 |
Total number of polymer chains | 4 |
Total formula weight | 241813.93 |
Authors | Safo, M.K.,Musayev, F.N.,Wu, S.H.,Abraham, D.J.,Ko, T.P. (deposition date: 2000-06-07, release date: 2000-06-21, Last modification date: 2024-02-07) |
Primary citation | Safo, M.K.,Musayev, F.N.,Wu, S.H.,Abraham, D.J.,Ko, T.P. Structure of tetragonal crystals of human erythrocyte catalase. Acta Crystallogr.,Sect.D, 57:1-7, 2001 Cited by PubMed Abstract: The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I4(1) by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6 A, yielding R and R(free) of 0.196 and 0.244, respectively, for all data at 2.4 A resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4(1)22 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes. PubMed: 11134921DOI: 10.1107/S0907444900013767 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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