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7ezp

Indole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase

Method: X-RAY DIFFRACTION Dmax: 112.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fructose-1,6-bisphosphatase 1

Homo sapiens

UniProt P09467

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–338 Chain B； UniProt 1–338 Chain C； UniProt 1–338 Chain D； UniProt 1–338 Not recorded FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 4 0GI 3-(3-hydroxy-3-oxopropyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.2M Ammonium acetate, 0.1M HEPES, 20% PEG 3350, pH 7.0 Resolution 2.80 Å R-free 0.256

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 7EZP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1FTA FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP Deposited 1993-09-27 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–337（337 aa）
Chain B 1–337（337 aa）
Chain C 1–337（337 aa）
Chain D 1–337（337 aa）
Not recorded AMP ADENOSINE MONOPHOSPHATE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å
2JJK FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR Deposited 2008-04-09 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded R15 N,N'-(heptane-1,7-diyldicarbamoyl)bis(3-chlorobenzenesulfonamide) × 2 X-RAY DIFFRACTION
X-ray crystallization conditions RESERVOIR = 0.1M HEPES PH7.0, 0.1M AMMONIUM ACETATE, 12% PEG 3350
Resolution 2.00 Å R-free 0.266
2VT5 FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR Deposited 2008-05-09 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded ROK 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions RESERVOIR = 0.1M HEPES, PH7.0, 0.1M AMMONIUM ACETATE, 12% PEG 3350
Resolution 2.20 Å R-free 0.247
2VT5 FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE -1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH A DUAL BINDING AMP SITE INHIBITOR Deposited 2008-05-09 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Chain G 1–338（338 aa）
Chain H 1–338（338 aa）
Not recorded ROK 4-AMINO-N-[(2-SULFANYLETHYL)CARBAMOYL]BENZENESULFONAMIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions RESERVOIR = 0.1M HEPES, PH7.0, 0.1M AMMONIUM ACETATE, 12% PEG 3350
Resolution 2.20 Å R-free 0.247
2WBB FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR Deposited 2009-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded RO3 N-{[(2Z)-5-BROMO-1,3-THIAZOL-2(3H)-YLIDENE]CARBAMOYL}-4-METHYLBENZENESULFONAMIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1M AMMONIUM ACETATE 0.1M HEPES PH7 25% PEG 3350
Resolution 2.22 Å R-free 0.248
2WBB FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR Deposited 2009-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Chain G 1–338（338 aa）
Chain H 1–338（338 aa）
Not recorded RO3 N-{[(2Z)-5-BROMO-1,3-THIAZOL-2(3H)-YLIDENE]CARBAMOYL}-4-METHYLBENZENESULFONAMIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1M AMMONIUM ACETATE 0.1M HEPES PH7 25% PEG 3350
Resolution 2.22 Å R-free 0.248
2WBD FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR Deposited 2009-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded RO5 N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-ethylbenzenesulfonamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1M AMMONIUM ACETATE, 0.1M HEPES PH 7.0, 15% PEG 3350
Resolution 2.40 Å R-free 0.277
2WBD FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE-1- PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH AN AMP SITE INHIBITOR Deposited 2009-02-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Chain G 1–338（338 aa）
Chain H 1–338（338 aa）
Not recorded RO5 N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-ethylbenzenesulfonamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions 0.1M AMMONIUM ACETATE, 0.1M HEPES PH 7.0, 15% PEG 3350
Resolution 2.40 Å R-free 0.277
2Y5K Orally active aminopyridines as inhibitors of tetrameric fructose 1,6- bisphosphatase Deposited 2011-01-14 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded YCU 1-[5-(2-METHOXYETHYL)-4-METHYL-THIOPHEN-2-YL]SULFONYL-3-[4-METHOXY-6-(METHYLCARBAMOYLAMINO)PYRIDIN-2-YL]UREA × 4 X-RAY DIFFRACTION
X-ray crystallization conditions RESERVOIR: 0.1M HEPES, PH 7.0, 0.1 M AMMONIUM ACETATE, 12% PEG 3350.
Resolution 2.10 Å R-free 0.296
2Y5L orally active aminopyridines as inhibitors of tetrameric fructose 1,6- bisphosphatase Deposited 2011-01-14 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded RO8 N-{[(2Z)-5-bromo-1,3-thiazol-2(3H)-ylidene]carbamoyl}-3-chlorobenzenesulfonamide × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.254
2Y5L orally active aminopyridines as inhibitors of tetrameric fructose 1,6- bisphosphatase Deposited 2011-01-14 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Chain G 1–338（338 aa）
Chain H 1–338（338 aa）
Not recorded RO8 N-{[(2Z)-5-bromo-1,3-thiazol-2(3H)-ylidene]carbamoyl}-3-chlorobenzenesulfonamide × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.254
3A29 Crystal structure of human liver FBPase in complex with tricyclic inhibitor Deposited 2009-05-08 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–338（337 aa）
Chain B 2–338（337 aa）
Chain C 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T0 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.60 Å R-free 0.247
3A29 Crystal structure of human liver FBPase in complex with tricyclic inhibitor Deposited 2009-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–338（337 aa）
Chain B 2–338（337 aa）
Not recorded 2T0 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.60 Å R-free 0.247
3A29 Crystal structure of human liver FBPase in complex with tricyclic inhibitor Deposited 2009-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–338（337 aa）
Chain C 2–338（337 aa）
Not recorded 2T0 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.60 Å R-free 0.247
3A29 Crystal structure of human liver FBPase in complex with tricyclic inhibitor Deposited 2009-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T0 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.60 Å R-free 0.247
3A29 Crystal structure of human liver FBPase in complex with tricyclic inhibitor Deposited 2009-05-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T0 2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.60 Å R-free 0.247
3KBZ Crystal structure of human liver FBPase in complex with tricyclic inhibitor 6 Deposited 2009-10-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–338（337 aa）
Chain B 2–338（337 aa）
Chain C 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T4 {[(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl}phosphonic acid × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.45 Å R-free 0.275
3KC0 Crystal structure of human liver FBPase in complex with tricyclic inhibitor 10b Deposited 2009-10-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–338（337 aa）
Chain B 2–338（337 aa）
Chain C 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T5 [(8H-indeno[1,2-d][1,3]thiazol-4-yloxy)methyl]phosphonic acid × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.80 Å R-free 0.254
3KC1 Crystal structure of human liver FBPase in complex with tricyclic inhibitor 19a Deposited 2009-10-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 2–338（337 aa）
Chain B 2–338（337 aa）
Chain C 2–338（337 aa）
Chain D 2–338（337 aa）
Not recorded 2T6 {[(7-carbamoyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl}phosphonic acid × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；8-10% PEG 3350, 0.15M NaCl, 0.1M Tris/HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 2.25 Å R-free 0.262
4MJO Human liver fructose-1,6-bisphosphatase(d-fructose-1,6-bisphosphate, 1-phosphohydrolase) (e.c.3.1.3.11) complexed with the allosteric inhibitor 3 Deposited 2013-09-04 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded 2C1 N-({4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl}carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M ammonium acetate and 12% polyethylenglycol 3350 in 0.1 M HEPES, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 2.40 Å R-free 0.236
4MJO Human liver fructose-1,6-bisphosphatase(d-fructose-1,6-bisphosphate, 1-phosphohydrolase) (e.c.3.1.3.11) complexed with the allosteric inhibitor 3 Deposited 2013-09-04 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Chain G 1–338（338 aa）
Chain H 1–338（338 aa）
Not recorded 2C1 N-({4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl}carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；300 K；0.1 M ammonium acetate and 12% polyethylenglycol 3350 in 0.1 M HEPES, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 2.40 Å R-free 0.236
5LDZ Quadruple space group ambiguity due to rotational and translational non-crystallographic symmetry in human liver fructose-1,6-bisphosphatase Deposited 2016-06-29 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded ZN ZINC ION × 6 SO4 SULFATE ION × 20 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCl pH 8.5, 2 M (NH4)2SO4
Resolution 2.20 Å R-free 0.239
5LDZ Quadruple space group ambiguity due to rotational and translational non-crystallographic symmetry in human liver fructose-1,6-bisphosphatase Deposited 2016-06-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain E 1–338（338 aa）
Chain F 1–338（338 aa）
Not recorded ZN ZINC ION × 6 SO4 SULFATE ION × 18 CL CHLORIDE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；295 K；0.1 M Tris-HCl pH 8.5, 2 M (NH4)2SO4
Resolution 2.20 Å R-free 0.239
6LW2 The N-arylsulfonyl-indole-2-carboxamide-based inhibitors against fructose-1,6-bisphosphatase Deposited 2020-02-07 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded EW0 7-chloranyl-4-[(3-methoxyphenyl)amino]-N-(4-methoxyphenyl)sulfonyl-1-methyl-indole-2-carboxamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M Ammonium acetate, 0.1M HEPES, 20% PEG 3350, pH 7.0
Resolution 2.40 Å R-free 0.290
7C9Q Crystal structure of Human liver fructose-1,6-bisphoaphatase complex with Mg2+ and AMP Deposited 2020-06-07 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded AMP ADENOSINE MONOPHOSPHATE × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；50mM Hepes pH 7.2, 150mM Sodium chloride, 8% (w/v) PEG 8000
Resolution 1.88 Å R-free 0.219
7CVH Human Fructose-1,6-bisphosphatase 1 in complex with geranylgeranyl diphosphate Deposited 2020-08-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 4 MG MAGNESIUM ION × 8 AMP ADENOSINE MONOPHOSPHATE × 4 GRG GERANYLGERANYL DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；28% (v/v) polyethylene glycol 600, 0.1M HEPES
Resolution 2.09 Å R-free 0.218
7CVN The N-arylsulfonyl-indole-2-carboxamide-based inhibitors against fructose-1,6-bisphosphatase Deposited 2020-08-26 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded GJO 4-(3-acetamidophenyl)-N-(4-methoxyphenyl)sulfonyl-7-nitro-1H-indole-2-carboxamide × 4 FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.2M Ammonium acetate, 0.1M HEPES, 20% PEG 3350, pH 7.0
Resolution 2.75 Å R-free 0.234
7CWE Human Fructose-1,6-bisphosphatase 1 in APO R-state Deposited 2020-08-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Not recorded MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.05 M cadmium sulfate, 0.1 M HEPES, pH 7.5, 1 M sodium acetate
Resolution 3.00 Å R-free 0.296
7EZF Indole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase Deposited 2021-06-01 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded 0KI 7-chloranyl-5-ethyl-3-(3-hydroxy-3-oxopropyl)-1H-indole-2-carboxylic acid × 4 FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.2M Ammonium acetate, 0.1M HEPES, 20% PEG 3350, pH 7.0
Resolution 2.76 Å R-free 0.236
7EZR Indole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase Deposited 2021-06-01 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Not recorded 0H1 5-ethyl-7-nitro-3-[3-oxidanylidene-3-(thiophen-2-ylsulfonylamino)propyl]-1H-indole-2-carboxylic acid × 4 FBP 1,6-di-O-phosphono-beta-D-fructofuranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.2M Ammonium acetate, 0.1M HEPES, 20% PEG 3350, pH 7.0
Resolution 3.27 Å R-free 0.253
7WVB Human Fructose-1,6-bisphosphatase 1 mutant R50A in APO R-state Deposited 2022-02-10 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–338（338 aa）
Chain B 1–338（338 aa）
Chain C 1–338（338 aa）
Chain D 1–338（338 aa）
Mutation：R50A Mutation：R50A Mutation：R50A Mutation：R50A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293.15 K；0.1M BIS-Tris(pH 6.5), 20% PEGMME 5000, 2.5% sucrose
Resolution 2.09 Å R-free 0.233
9XV1 Crystal Structure of Fructose-1,6-bisphosphatase Complexed with a Covalent Inhibitor Deposited 2025-11-25 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–336（336 aa）
Chain B 1–336（336 aa）
Chain C 1–336（336 aa）
Chain D 1–336（336 aa）
Not recorded A1E1G 2-bromanyl-~{N}-[2-[4-[(3-phenylphenyl)carbamoylsulfamoyl]phenyl]ethyl]ethanamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris (pH 8.8), 15% (v/v) EtOH
Resolution 1.96 Å R-free 0.213

22 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F16P1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–338； UniProt 1–338 Author chain B； PDBConstruct 1–338； UniProt 1–338 Author chain C； PDBConstruct 1–338； UniProt 1–338 Author chain D； PDBConstruct 1–338； UniProt 1–338

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 7ezp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ezp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ezp
Deposition date deposition_date2021-06-01
Structure title titleIndole-2-carboxylic acid derivatives as allosteric inhibitors of fructose-1,6-bisphosphatase
Keywords keywordsfructose-1, 6-bisphosphatase, indole dicarboxylic acid derivatives, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.15 Å
Radius of gyration Rg (electron density) rg_electron33.63 Å
Forward intensity I(0) i0598727000.00
Molecular weight molecular_weight131850.0 kDa
Excluded volume excluded_volume127180 ų
Envelope volume envelope_volume212870 ų
Hydration-shell volume shell_volume51236 ų
Envelope diameter envelope_diameter118.7 Å
Shell Rg shell_rg41.42 Å
Envelope Rg envelope_rg33.85 Å
Shape Rg shape_rg33.66 Å
Total Rg total_rg33.96 Å
Total atoms total_atoms9941
Residues n_residues1279
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax112.8 Å
Rg (real space) rg_real34.09 Å
Rg uncertainty (real space) rg_real_error0.74 Å
I(0) (real space) i0_real5.9870e+08
I(0) uncertainty (real space) i0_real_error9.7120e+06
Rg (reciprocal space) rg_reciprocal34.13 Å
I(0) (reciprocal space) i0_reciprocal598700000.0000
Solution quality estimate total_estimate0.8901
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.7 Å
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.2300 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha430000000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.927
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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8. Citations (1)

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9. Files and Curves (10)