Crystal structure of Cytochrome c Peroxidase with a Proposed Electron Transfer Pathway Excised to Form a Ligand Binding Channel.
The structure was published by Rosenfeld, R.J., Hays, A.M., Musah, R.A., and Goodin, D.B., in 2002 in a paper entitled "Excision of a proposed electron transfer pathway in cytochrome c peroxidase and its replacement by a ligand-binding channel." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.74 Å and deposited in 2002.
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 290 residues which is < 90% of the natural sequence. Out of 290 residues 287 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: