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Structure paper

TitleCrystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities.
Journal, issue, pagesJ. Biol. Chem., Vol. 274, Page 2176-2184, Year 1999
Publish dateOct 26, 1998 (structure data deposition date)
AuthorsYuen, M.H. / Mizuguchi, H. / Lee, Y.H. / Cook, P.F. / Uyeda, K. / Hasemann, C.A.
External linksJ. Biol. Chem. / PubMed:9890980
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-2bif:
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE H256A MUTANT WITH F6P IN PHOSPHATASE ACTIVE SITE
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-BOG:
octyl beta-D-glucopyranoside / detergent*YM

ChemComp-F6P:
6-O-phosphono-beta-D-fructofuranose

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-SIN:
SUCCINIC ACID

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / HYDROLASE / KINASE / TRANSFERASE (PHOSPHO) / PHOSPHATASE / HYDROLASE (PHOSPHO) / GLYCOLYSIS / BIFUNCTIONAL ENZYME

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