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Structure paper

TitleCharge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes.
Journal, issue, pagesProtein Sci., Vol. 26, Page 2221-2228, Year 2017
Publish dateApr 28, 2017 (structure data deposition date)
AuthorsEndrizzi, J.A. / Beernink, P.T.
External linksProtein Sci. / PubMed:28833948
MethodsX-ray diffraction
Resolution2.012 Å
Structure data

PDB-5vmq:
STRUCTURE OF THE R105A MUTANT CATALYTIC TRIMER OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE AT 2.0-A RESOLUTION
Method: X-RAY DIFFRACTION / Resolution: 2.012 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli o45:k1 (strain s88 / expec) (bacteria)
KeywordsTRANSFERASE / Rossman fold / Mutant / Pyrimidine biosynthesis / Aspartate carbamoyltransferase

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