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TitleThe putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase.
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 26952-26957, Year 2003
Publish dateApr 24, 2003 (structure data deposition date)
AuthorsPruett, P.S. / Azzi, A. / Clark, S.A. / Yousef, M.S. / Gattis, J.L. / Somasundaram, T. / Ellington, W.R. / Chapman, M.S.
External linksJ. Biol. Chem. / PubMed:12732621
MethodsX-ray diffraction
Resolution1.9 - 2.8 Å
Structure data

PDB-1p50:
Transition state structure of an Arginine Kinase mutant
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1p52:
Structure of Arginine kinase E314D mutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MG:
Unknown entry

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

ChemComp-NO3:
NITRATE ION

ChemComp-ARG:
ARGININE

ChemComp-HOH:
WATER

ChemComp-DAR:
D-ARGININE

Source
  • limulus polyphemus (Atlantic horseshoe crab)
KeywordsTRANSFERASE / phosphagen kinase / transition state / ARGININE KINASE / TRANSITION STATE ANALOG / ADENOSINE TRI-PHOSPHATE

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