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3D structures from the PDB for "Fructose-1,6-bisphosphatase 1 (FBPase)" AND "BDBM18137"
(Proteins have >= 85% sequence identity and ligands are exact matches)


Seq IdentityJmol DisplayPDB Title
1NV7100%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6-PHOSPHATE, PHOSPHATE AND THALLIUM (20 MM)
1EYK100%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6- PHOSPHATE AND PHOSPHATE (T-STATE)
1EYJ100%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6- PHOSPHATE AND PHOSPHATE (T-STATE)
2F3D>99%JmolMECHANISM OF DISPLACEMENT OF A CATALYTICALLY ESSENTIAL LOOP FROM THE ACTIVE SITE OF FRUCTOSE-1,6-BISPHOSPHATASE
1YZ0>99%JmolR-STATE AMP COMPLEX REVEALS INITIAL STEPS OF THE QUATERNARY TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE
1YYZ>99%JmolR-STATE AMP COMPLEX REVEALS INITIAL STEPS OF THE QUATERNARY TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE
1FJ9>99%JmolFRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T- STATE)
1KZ8>99%JmolCRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR
1FPF>99%JmolSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6- BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2, 5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
1FPE>99%JmolSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6- BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2, 5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
1FPD>99%JmolSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6- BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2, 5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
1FBP>99%JmolCRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE 6-PHOSPHATE, AMP, AND MAGNESIUM
1FPG>99%JmolSTRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6- BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2, 5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY
1FPI>99%JmolFRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1- PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6- BISPHOSPHATE AND POTASSIUM IONS (100 MM)
1FPJ>99%JmolFRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1- PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6- BISPHOSPHATE, THALLIUM (10 MM) AND LITHIUM IONS (10 MM)
1FPL>99%JmolFRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1- PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6- BISPHOSPHATE AND THALLIUM IONS (10 MM)
4FBP>99%JmolCONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)
1RDZ99%JmolT-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
1RDY99%JmolT-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
1FSA99%JmolTHE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI
1FRP99%JmolCRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-2,6-BISPHOSPHATE, AMP AND ZN2+ AT 2.0 ANGSTROMS RESOLUTION. ASPECTS OF SYNERGISM BETWEEN INHIBITORS
1FTA91%JmolFRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP