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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
Resolution1.28 - 2.1 Å
Structure data

PDB-4jex:
Y21K mutant of N-acetylornithine aminotransferase complexed with L-canaline
Method: X-RAY DIFFRACTION / Resolution: 1.43 Å

PDB-4jey:
E198A mutant of N-acetylornithine aminotransferase from Salmonella typhimurium
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4jez:
N79R mutant of N-acetylornithine aminotransferase complexed with L-canaline
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-4jf0:
N79R mutant of N-acetylornithine aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4jf1:
R144Q mutant of N-acetylornithine aminotransferase
Method: X-RAY DIFFRACTION / Resolution: 1.28 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACT:
ACETATE ION

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

ChemComp-NA:
Unknown entry

ChemComp-TNF:
PICRIC ACID

ChemComp-HOH:
WATER

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

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

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