2oat
From Proteopedia
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ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE
Overview
Ornithine aminotransferase (l-ornithine:2-oxoacid delta-aminotransferase;, EC 2.6.1.13), a pyridoxal-5'-phosphate-dependent mitochondrial enzyme, controls the l-ornithine level in tissues by catalyzing the transfer of, the delta-amino group of l-ornithine to 2-oxoglutarate, producing, l-glutamate- gamma-semialdehyde and l-glutamate. (2S, 5S)-5-Fluoromethylornithine is the only inhibitor exclusively specific for, ornithine aminotransferase known to date. Both in vitro and in vivo, it, blocks the enzyme by a suicide reaction leading to a covalent adduct with, the cofactor. The crystal structure of the enzyme-inhibitor complex was, solved at a resolution of 1.95 A. No significant conformational changes, compared with the native enzyme structure were observed. The structure, reveals the ... [(full description)]
About this Structure
2OAT is a [Single protein] structure of sequence from [Homo sapiens] with PFM as [ligand]. Active as [[1]], with EC number [2.6.1.13]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine., Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN, J Mol Biol. 1999 Jan 8;285(1):297-309. PMID:9878407
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