1oc3: Difference between revisions
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Revision as of 16:44, 30 October 2007
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HUMAN PEROXIREDOXIN 5
OverviewOverview
Peroxiredoxin 5 is the last discovered mammalian member of an ubiquitous, family of peroxidases widely distributed among prokaryotes and eukaryotes., Mammalian peroxiredoxin 5 has been recently classified as an atypical, 2-Cys peroxiredoxin due to the presence of a conserved peroxidatic, N-terminal cysteine (Cys47) and an unconserved resolving C-terminal, cysteine residue (Cys151) forming an intramolecular disulfide intermediate, in the oxidized enzyme. We have recently reported the crystal structure of, human peroxiredoxin 5 in its reduced form. Here, a new crystal form of, human peroxiredoxin 5 is described at 2.0 A resolution. The asymmetric, unit contains three polypeptide chains. Surprisingly, beside two reduced, chains, the third one is oxidized although the enzyme was crystallized, ... [(full description)]
About this StructureAbout this Structure
1OC3 is a [Single protein] structure of sequence from [Homo sapiens] with BEZ as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of a dimeric oxidized form of human peroxiredoxin 5., Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP, J Mol Biol. 2004 Apr 9;337(5):1079-90. PMID:15046979
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