ROLE OF MET-230 IN INTRAMOLECULAR ELECTRON TRANSFER BETWEEN THE OXYFERRYL HEME AND TRP 191 IN CYTOCHROME C PEROXIDASE COMPOUND II
The structure was published by Liu, R.Q., Miller, M.A., Han, G.W., et al., Kraut, J., Durham, B., and Millett, F., in 1994 in a paper entitled "Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.
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 296 residues which is < 90% of the natural sequence. Out of 296 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: