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C153S MUTANT OF PEA FRUCTOSE-1,6-BISPHOSPHATASE[HYDROLASE]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE[HYDROLASE]
OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATASE FORM 1[HYDROLASE]
Human muscle fructose-1,6-bisphosphatase E69Q mutant in complex with AMP and alpha fructose-6-phosphate[HYDROLASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
Human muscle fructose-1,6-bisphosphatase E69Q mutant in complex with AMP[HYDROLASE]
E. coli Fructose-1,6-bisphosphatase: Citrate, Fru-2,6-P2, and Mg2+ bound[HYDROLASE]
T-like Fructose-1,6-bisphosphatase from Escherichia coli with AMP, Glucose 6-phosphate, and Fructose 1,6-bisphosphate bound[HYDROLASE]
R-state, PEP and Fru-6-P-bound, Escherichia coli fructose-1,6-bisphosphatase[HYDROLASE]
R-state, citrate and Fru-6-P-bound Escherichia coli fructose-1,6-bisphosphatase[HYDROLASE]
Crystal Structure of Recombinant Type I Fructose-1,6-bisphosphatase from Escherichia coli Complexed with Sulfate Ions[HYDROLASE]
CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION[HYDROLASE (PHOSPHORIC MONOESTER)]
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CRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR[HYDROLASE]
Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase[HYDROLASE]
CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION[HYDROLASE]
CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH THE PRODUCT FRUCTOSE 6-PHOSPHATE AT 2.1-ANGSTROMS RESOLUTION[HYDROLASE (PHOSPHORIC MONOESTER)]
CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)[HYDROLASE (PHOSPHORIC MONOESTER)]
STRUCTURE REFINEMENT OF FRUCTOSE-1,6-BISPHOSPHATASE AND ITS FRUCTOSE 2,6-BISPHOSPHATE COMPLEX AT 2.8 ANGSTROMS RESOLUTION[HYDROLASE (PHOSPHORIC MONOESTER)]
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