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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P0AB71 New Search
11PDB entries
14Biological assembly
27chain/assembly records
Main Difference Dimensions in This Set
Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1B57 CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE IN COMPLEX WITH PHOSPHOGLYCOLOHYDROXAMATE Deposited 1999-01-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–358（358 aa）
Chain B 1–358（358 aa）
Not recorded ZN ZINC ION × 7 NA SODIUM ION × 2 CL CHLORIDE ION × 1 PGH PHOSPHOGLYCOLOHYDROXAMIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；pH 7.5
Resolution 2.00 Å R-free 0.230
1DOS STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE Deposited 1996-06-24 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–358（358 aa）
Chain B 1–358（358 aa）
Not recorded ZN ZINC ION × 2 NH4 AMMONIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；pH 5.5
Resolution 1.67 Å R-free 0.204
1ZEN CLASS II FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE Deposited 1996-07-08 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–358（358 aa）
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.326
5GK3 Native structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.8 Angstrom resolution Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded GOL GLYCEROL × 3 ZN ZINC ION × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 5% fructose 1,6-bisphosphatase, 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 1.80 Å R-free 0.189
5GK4 Native structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 2.0 Angstrom resolution Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded GOL GLYCEROL × 2 ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 5% fructose 1,6-bisphosphatase, 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 2.00 Å R-free 0.200
5GK5 Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded GOL GLYCEROL × 2 ZN ZINC ION × 3 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 1mM Docosahexaenoic acid , 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 1.90 Å R-free 0.207
5GK5 Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution Deposited 2016-07-03 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 1–359（359 aa）
Chain D 1–359（359 aa）
Not recorded GOL GLYCEROL × 2 ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 1mM Docosahexaenoic acid , 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 1.90 Å R-free 0.207
5GK5 Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution Deposited 2016-07-03 Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 1–359（359 aa）
Chain F 1–359（359 aa）
Not recorded GOL GLYCEROL × 1 ZN ZINC ION × 3 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 1mM Docosahexaenoic acid , 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 1.90 Å R-free 0.207
5GK5 Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution Deposited 2016-07-03 Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 1–359（359 aa）
Chain H 1–359（359 aa）
Not recorded GOL GLYCEROL × 2 ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 1mM Docosahexaenoic acid , 0.1M Tris pH 7.0, and 15% PEG 4000
Resolution 1.90 Å R-free 0.207
5GK6 Structure of E.Coli fructose 1,6-bisphosphate aldolase, Citrate bound form Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded ZN ZINC ION × 2 CIT CITRIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2M ammonium acetate, 5mM aldose, 0.1M citrate buffer pH 7.0, and 15% PEG 4000
Resolution 1.80 Å R-free 0.194
5GK7 Structure of E.Coli fructose 1,6-bisphosphate aldolase bound to Tris Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded GOL GLYCEROL × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2 M ammonium acetate, 5mM fructose 1,6-bisphosphatase, 0.1 M Tris/HCl pH 7.0, and 15% PEG 4000
Resolution 1.80 Å R-free 0.197
5GK8 Structure of E.Coli fructose 1,6-bisphosphate aldolase, Acetate bound form Deposited 2016-07-03 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–359（359 aa）
Chain B 1–359（359 aa）
Not recorded GOL GLYCEROL × 4 ACT ACETATE ION × 2 ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；287 K；0.2 M ammonium acetate, 5% fructose 1,6-bisphosphatase, 0.1 M Tris pH 7.0, and 15% PEG 4000
Resolution 2.00 Å R-free 0.200
5VJD Class II fructose-1,6-bisphosphate aldolase of Escherichia coli with DHAP Deposited 2017-04-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 2–359（358 aa）
Chain B 2–359（358 aa）
Not recorded NA SODIUM ION × 4 ZN ZINC ION × 2 13P 1,3-DIHYDROXYACETONEPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；PEG 4000, MgCl2, Hepes buffer
Resolution 1.70 Å R-free 0.172
5VJE Class II fructose-1,6-bisphosphate aldolase of Escherichia coli with D-glucitol 1,6-bisphosphate Deposited 2017-04-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 2–359（358 aa）
Chain B 2–359（358 aa）
Not recorded NA SODIUM ION × 4 GOS D-Glucitol-1,6-bisphosphate × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；PEG 4000, MgCl2, Hepes buffer
Resolution 1.65 Å R-free 0.164

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.