Stabilization of the Engineered Cation-binding Loop in Cytochrome c Peroxidase (CcP)
The structure was published by Bhaskar, B., Bonagura, C.A., Li, H., and Poulos, T.L., in 2002 in a paper entitled "Cation-induced stabilization of the engineered cation-binding loop in cytochrome c peroxidase (CcP)." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2001.
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 294 residues which is < 90% of the natural sequence. Out of 294 residues 294 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: