1cca Summary

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THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME

The structure was published by Goodin, D.B. and McRee, D.E., in 1993 in a paper entitled "The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.

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)search. The sample contained 297 residues which is < 90% of the natural sequence. Out of 297 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CYTOCHROME C PEROXIDASE P00431 (68-361) (CCPR_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 297 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00431 (68 - 361) CYTOCHROME C PEROXIDASE Saccharomyces cerevisiae

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A CCP-likesearch Peroxidase; domain 1search, Peroxidase, domain 2search Peroxidasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P00431) heme bindingsearch peroxidase activitysearch response to oxidative stresssearch oxidation-reduction processsearch

Chain InterPro annotation
A Haem peroxidase, plant/fungal/bacterialsearch Plant ascorbate peroxidasesearch Haem peroxidasesearch Peroxidases heam-ligand binding sitesearch Peroxidase, active sitesearch