1CCC
THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME
Summary for 1CCC
Entry DOI | 10.2210/pdb1ccc/pdb |
Descriptor | CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Cellular location | Mitochondrion matrix: P00431 |
Total number of polymer chains | 1 |
Total formula weight | 34459.21 |
Authors | Goodin, D.B.,Mcree, D.E. (deposition date: 1993-01-04, release date: 1993-10-31, Last modification date: 2024-02-07) |
Primary citation | Goodin, D.B.,McRee, D.E. The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry, 32:3313-3324, 1993 Cited by PubMed: 8384877DOI: 10.1021/bi00064a014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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