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


Seq IdentityJmol DisplayPDB Title
1FRP 0%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 10.1073/PNAS.91.26.12482
1FPL 0%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) 10.1073/PNAS.92.19.8916
1FPJ 0%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) 10.1073/PNAS.92.19.8916
1FPI 0%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) 10.1073/PNAS.92.19.8916
1FPG 0%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 10.1021/BI00013A020
1FPF 0%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 10.1021/BI00013A020
1FPE 0%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 10.1021/BI00013A020
1FPD 0%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 10.1021/BI00013A020
1FJ9 0%JmolFRUCTOSE-1,6-BISPHOSPHATASE (MUTANT Y57W) PRODUCTS/ZN/AMP COMPLEX (T- STATE) 10.1021/BI000609C
1FBP 0%JmolCRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE 6-PHOSPHATE, AMP, AND MAGNESIUM 10.1073/PNAS.87.14.5243
1EYK 0%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, ZINC, FRUCTOSE-6- PHOSPHATE AND PHOSPHATE (T-STATE) 10.1021/BI000574G
1EYJ 0%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6- PHOSPHATE AND PHOSPHATE (T-STATE) 10.1021/BI000574G
1FSA 0%JmolTHE T-STATE STRUCTURE OF LYS 42 TO ALA MUTANT OF THE PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI No DOI
1FTA 0%JmolFRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP No DOI
1KZ8 0%JmolCRYSTAL STRUCTURE OF PORCINE FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH A NOVEL ALLOSTERIC-SITE INHIBITOR 10.1021/JM010496A
1NV7 0%JmolFRUCTOSE-1,6-BISPHOSPHATASE COMPLEX WITH AMP, MAGNESIUM, FRUCTOSE-6-PHOSPHATE, PHOSPHATE AND THALLIUM (20 MM) 10.1074/JBC.M212394200
1RDY 0%JmolT-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI No DOI
1RDZ 0%JmolT-STATE STRUCTURE OF THE ARG 243 TO ALA MUTANT OF PIG KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE EXPRESSED IN E. COLI No DOI
1YYZ 0%JmolR-STATE AMP COMPLEX REVEALS INITIAL STEPS OF THE QUATERNARY TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE 10.1074/JBC.M501011200
1YZ0 0%JmolR-STATE AMP COMPLEX REVEALS INITIAL STEPS OF THE QUATERNARY TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE 10.1074/JBC.M501011200
2F3D 0%JmolMECHANISM OF DISPLACEMENT OF A CATALYTICALLY ESSENTIAL LOOP FROM THE ACTIVE SITE OF FRUCTOSE-1,6-BISPHOSPHATASE 10.1021/BI400532N
4FBP 0%JmolCONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM) 10.1021/BI00232A007