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TitleStructure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases
Journal, issue, pagesProtein Sci., Vol. 20, Page 557-566, Year 2011
Publish dateJun 4, 2009 (structure data deposition date)
AuthorsPai, C.-H. / Wu, H.-J. / Lin, C.-H. / Wang, A.H.-J.
External linksProtein Sci. / PubMed:21226054
MethodsX-ray diffraction
Resolution1.95 - 2.8 Å
Structure data

PDB-3a2y:
E. coli Gsp amidase C59A complexed with Gsp
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3o98:
Glutathionylspermidine synthetase/amidase C59A complex with ADP and Gsp
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-TS5:
GLUTATHIONYLSPERMIDINE

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsHydrolase / Ligase / Gsp amidase / ATP-binding / Multifunctional enzyme / Nucleotide-binding

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