1bek Summary

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EFFECT OF UNNATURAL HEME SUBSTITUTION ON KINETICS OF ELECTRON TRANSFER IN CYTOCHROME C PEROXIDASE

A publication describing this structure is not available. The depositing authors are Miller, M.A.search; Kraut, J.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of YEAST CYTOCHROME C PEROXIDASE. This molecule has the UniProt identifier P00431 (CCPR_YEAST)search. The sample contained 291 residues which is < 90% of the natural sequence. Out of 291 residues 286 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 YEAST CYTOCHROME C PEROXIDASE P00431 (71-361) (CCPR_YEAST)search Saccharomyces cerevisiae S288csearch < 90% 291 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00431 (71 - 361) YEAST 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 Biological process (GO) Molecular function (GO)
A (P00431) oxidation-reduction processsearch response to oxidative stresssearch heme bindingsearch peroxidase activitysearch

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