SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (INDOLINE)
The structure was published by Musah, R.A., Jensen, G.M., Bunte, S.W., Rosenfeld, R.J., and Goodin, D.B., in 2002 in a paper entitled "Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein." (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: