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Structure paper

TitleThe crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Journal, issue, pagesNat. Struct. Biol., Vol. 3, Page 74-86, Year 1996
Publish dateApr 4, 1995 (structure data deposition date)
AuthorsTesmer, J.J. / Klem, T.J. / Deras, M.L. / Davisson, V.J. / Smith, J.L.
External linksNat. Struct. Biol. / PubMed:8548458
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-1gpm:
ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-POP:
PYROPHOSPHATE 2-

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-CIT:
CITRIC ACID

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE (GLUTAMINE AMIDOTRANSFERASE) / CLASS I GLUTAMINE AMIDOTRANSFERASE / N-TYPE ATP PYROPHOSPHATASE

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