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Structure paper

TitleConformational transitions, ligand specificity and catalysis in N-acetylornithine aminotransferase: Implications on drug designing and rational enzyme engineering in omega aminotransferases.
Journal, issue, pagesTo be Published
Publish dateFeb 27, 2013 (structure data deposition date)
AuthorsBisht, S. / Bharath, S.R. / Murthy, M.R.N.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.48 - 1.67 Å
Structure data

PDB-4jev:
N-acetylornithine aminotransferase from S. typhimurium complexed with gabaculine
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-4jew:
N-acetylornithine aminotransferase from S. typhimurium complexed with L-canaline
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

Chemicals

ChemComp-PXG:
3-[O-PHOSPHONOPYRIDOXYL]--AMINO-BENZOIC ACID

ChemComp-ACT:
ACETATE ION

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-P00:
(2S)-2-azanyl-4-[(E)-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]oxy-butanoic acid

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-TNF:
PICRIC ACID

Source
  • salmonella typhimurium (bacteria)
KeywordsTRANSFERASE / PLP dependent fold type I subclass II aminotransferase / PLP dependent fold type I sub class II aminotransferase

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