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
The structure was published by Goodin, D.B. and McRee, D.E., in 1993 in a paper entitled "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." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CYTOCHROME C PEROXIDASE. This molecule has the UniProt identifier P00431 (CCPR_YEAST). The sample contained 297 residues which is < 90% of the natural sequence. Out of 297 residues 290 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: