1vz5

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File:1vz5.gif


1vz5, resolution 2.15Å

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SUCCINATE COMPLEX OF ATSK

OverviewOverview

The alkylsulfatase AtsK from Pseudomonas putida S-313 is a member of the, non-heme iron(II)-alpha-ketoglutarate-dependent dioxygenase superfamily., In the initial step of their catalytic cycle, enzymes belonging to this, widespread and versatile family coordinate molecular oxygen to the iron, center in the active site. The subsequent decarboxylation of the, cosubstrate alpha-ketoglutarate yields carbon dioxide, succinate, and a, highly reactive ferryl (IV) species, which is required for substrate, oxidation via a complex mechanism involving the transfer of radical, species. Non-productive activation of oxygen may lead to harmful side, reactions; therefore, such enzymes need an effective built-in protection, mechanism. One of the ways of controlling undesired side reactions is the, ... [(full description)]

About this StructureAbout this Structure

1VZ5 is a [Single protein] structure of sequence from [Pseudomonas putida] with SIN as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Succinate complex crystal structures of the alpha-ketoglutarate-dependent dioxygenase AtsK: steric aspects of enzyme self-hydroxylation., Muller I, Stuckl C, Wakeley J, Kertesz M, Uson I, J Biol Chem. 2005 Feb 18;280(7):5716-23. Epub 2004 Nov 12. PMID:15542595

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