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TitleThe 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase from the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms that This Thermoestable Enzyme is a Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases
Journal, issue, pagesJ. Mol. Biol., Vol. 299, Page 463-, Year 2000
Publish dateApr 28, 2000 (structure data deposition date)
AuthorsRamon-Maiques, S. / Marina, A. / Uriarte, M. / Fita, I. / Rubio, V.
External linksJ. Mol. Biol. / PubMed:10860751
MethodsX-ray diffraction
Resolution1.5 Å
Structure data

PDB-1e19:
Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • pyrococcus furiosus (archaea)
KeywordsTRANSFERASE / HYPERTHERMOPHILES / ADP SITE / ARGININE METABOLISM PHOSPHORYL GROUP TRANSFER

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