1hch Summary



The structure was published by Berglund, G.I., Carlsson, G.H., Smith, A.T., Szoke, H., Henriksen, A., and Hajdu, J., in 2002 in a paper entitled "The Catalytic Pathway of Horseradish Peroxidase at High Resolution" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.57 Å and deposited in 2001.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PEROXIDASE C1A. This molecule has the UniProt identifier P00433 (PER1A_ARMRU)search. The sample contained 306 residues which is 95% of the natural sequence. Out of 306 residues 305 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 PEROXIDASE C1A P00433 (31-336) (PER1A_ARMRU)search Armoracia rusticanasearch 95% 306 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00433 (31 - 336) PEROXIDASE C1A Armoracia rusticana

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00433) CCP-likesearch Peroxidase; domain 1search, Peroxidase, domain 2search PF00141: Peroxidasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00433) heme bindingsearch peroxidase activitysearch metal ion bindingsearch oxidoreductase activitysearch oxidation-reduction processsearch response to oxidative stresssearch hydrogen peroxide catabolic processsearch vacuolesearch extracellular regionsearch

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