Editing Ornithine decarboxylase (section)

== Structure ==
[[image:Ornithine Decarboxylase Publication View.png|270px|thumb|right|3D crystal structure of ornithine decarboxylase.<ref name="pmid10623504">{{PDB|1d7k}}; {{cite journal | vauthors = Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML | title = Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding | journal = Journal of Molecular Biology | volume = 295 | issue = 1 | pages = 7–16 | date = January 2000 | pmid = 10623504 | doi = 10.1006/jmbi.1999.3331 }}; rendered via [http://pymol.sourceforge.net PyMOL].</ref>]]

The active form of ornithine decarboxylase is a [[homodimer]]. Each [[monomer]] contains a barrel domain, consisting of an [[Alpha beta barrel|alpha-beta barrel]], and a sheet domain, composed of two [[beta-sheet]]s. The domains are connected by loops. The monomers connect to each other via interactions between the barrel of one monomer and the sheet of the other. Binding between monomers is relatively weak, and ODC interconverts rapidly between monomeric and dimeric forms in the cell.<ref name="pmid10378276"/>

The [[pyridoxal phosphate]] cofactor binds lysine 69 at the [[C-terminus]] end of the barrel domain.  The [[active site]] is at the interface of the two domains, in a cavity formed by loops from both monomers.<ref name="pmid10378276"/>