INTRODUCTION OF NOVEL SUBSTRATE OXIDATION INTO CYTOCHROME C PEROXIDASE BY CAVITY COMPLEMENTATION: OXIDATION OF 2-AMINOTHIAZOLE AND COVALENT MODIFICATION OF THE ENZYME (2-AMINOTHIAZOLE)
The structure was published by Musah, R.A. and Goodin, D.B., in 1997 in a paper entitled "Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1997.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of CYTOCHROME C PEROXIDASE. This molecule has the UniProt identifier P00431 (CCPR_YEAST). The sample contained 294 residues which is < 90% of the natural sequence. Out of 294 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: