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TitleL-allo-Threonine aldolase with an H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 70, Page 1695-1703, Year 2014
Publish dateAug 3, 2013 (structure data deposition date)
AuthorsQin, H.M. / Imai, F.L. / Miyakawa, T. / Kataoka, M. / Kitamura, N. / Urano, N. / Mori, K. / Kawabata, H. / Okai, M. / Ohtsuka, J. ...Qin, H.M. / Imai, F.L. / Miyakawa, T. / Kataoka, M. / Kitamura, N. / Urano, N. / Mori, K. / Kawabata, H. / Okai, M. / Ohtsuka, J. / Hou, F. / Nagata, K. / Shimizu, S. / Tanokura, M.
External linksActa Crystallogr. ,Sect. D / PubMed:24914980
MethodsX-ray diffraction
Resolution2.5 - 2.6 Å
Structure data

PDB-3wgb:
Crystal structure of aeromonas jandaei L-allo-threonine aldolase
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3wgc:
Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-PLG:
N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE]

ChemComp-GLY:
GLYCINE

ChemComp-HOH:
WATER

Source
  • aeromonas jandaei (bacteria)
KeywordsLYASE / PYRIDOXAL-5'-PHOSPHATE / threonine aldolase

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