1sch

Revision as of 18:14, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1sch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sch, resolution 2.56Å" /> '''PEANUT PEROXIDASE''...)
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PEANUT PEROXIDASE

File:1sch.gif


1sch, resolution 2.56Å

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OverviewOverview

BACKGROUND. Peroxidases catalyze a wide variety of peroxide-dependent, oxidations. Based on sequence alignments, heme peroxidases have been, divided into three classes. Crystal structures are available for, peroxidases of classes I and II, but until now no structure has been, determined for class III, the classical extracellular plant peroxidases., RESULTS. The crystal structure of peanut peroxidase has been solved to 2.7, A resolution. The helical fold is similar to that of known peroxidase, structures. The 294-residue polypeptide chain is accompanied by a heme and, two calcium ions, and there is some evidence of glycosylation., CONCLUSIONS. This is the first complete structure of a class III, peroxidase and as such should serve as a model for other class III enzymes, including the ... [(full description)]

About this StructureAbout this Structure

1SCH is a [Single protein] structure of sequence from [[1]] with NAG, CA and HEM as [ligands]. Active as [[2]], with EC number [1.11.1.7]. Full crystallographic information is available from [OCA].

ReferenceReference

The crystal structure of peanut peroxidase., Schuller DJ, Ban N, Huystee RB, McPherson A, Poulos TL, Structure. 1996 Mar 15;4(3):311-21. PMID:8805539

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