EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of YEAST CYTOCHROME C PEROXIDASE. This molecule has the UniProt identifier P00431 (CCPR_YEAST). The sample contained 291 residues which is < 90% of the natural sequence. Out of 291 residues 286 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: