3dft

Phosphate ions in D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle

Method: X-RAY DIFFRACTION D_max: 112.2 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fructose-bisphosphate aldolase A

Oryctolagus cuniculus

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 2–364 Chain B； UniProt 2–364 Chain C； UniProt 2–364 Chain D； UniProt 2–364	Mutation：D33S	PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.94 Å R-free 0.205

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 3DFT	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
11NH Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.42 Å
11NI Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.27 Å
11NJ Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.40 Å
11NK Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.17 Å
11NL Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.5x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.41 Å
11NM Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.5x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.19 Å
11NN Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.34 Å
11NO Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.10 Å
11NP Rabbit muscle Aldolase (C1 symmetry) determined using the SPT Labtech chameleon (gold-coated grids) in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.43 Å
11NR Rabbit muscle Aldolase (D2 symmetry) determined using the SPT Labtech chameleon (gold-coated grids) in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon	Resolution 2.17 Å
11NT Rabbit muscle Aldolase (C1 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 0x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the TFS Vitrobot Mark IV	Resolution 2.25 Å
11NU Rabbit muscle Aldolase (D2 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 0x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the TFS Vitrobot Mark IV	Resolution 1.97 Å
11NW Rabbit muscle Aldolase (C1 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the TFS Vitrobot Mark IV	Resolution 2.16 Å
11NX Rabbit muscle Aldolase (D2 symmetry) determined using the TFS Vitrobot Mark IV in the presence of 1x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the TFS Vitrobot Mark IV	Resolution 1.98 Å
11OB Rabbit muscle Aldolase (C1 symmetry) determined using a manually-operated plunging device in the presence of 0.25x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；Samples were frozen using a manually-operated plunging device	Resolution 2.38 Å
11OC Rabbit muscle Aldolase (D2 symmetry) determined using a manually-operated plunging device in the presence of 0.25x SurfACT Deposited 2026-03-05	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；Samples were frozen using a manually-operated plunging device	Resolution 2.18 Å
1ADO FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE Deposited 1996-12-02	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Not recorded	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；RABBIT MUSCLE ALDOLASE WAS CRYSTALLIZED FROM A 42% SATURATED AMMONIUM SULFATE SOLUTION, pH 7.5	Resolution 1.90 Å R-free 0.203
1EWD FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE Deposited 2000-04-25	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Mutation：K107M Mutation：K107M Mutation：K107M Mutation：K107M	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.4；293 K；Ammonium sulfate 43%, EDTA 5mM, TRIETHYLAMINE 100mM, pH 7.4, SMALL TUBES, temperature 293K	Resolution 2.46 Å R-free 0.234
1EWE Fructose 1,6-Bisphosphate Aldolase from Rabbit Muscle Deposited 2000-04-25	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Mutation：K107M Mutation：K107M Mutation：K107M Mutation：K107M	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.4；293 K；Ammonium sulfate, 43 percent 5mM EDTA, pH 7.4, SMALL TUBES, temperature 293K	Resolution 2.60 Å R-free 0.237
1EX5 FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE Deposited 2000-04-25	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Mutation：E187A Mutation：E187A Mutation：E187A Mutation：E187A	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.4；293 K；40% ammonium sulphate, 5mM EDTA, pH 7.4, SMALL TUBES, temperature 293K	Resolution 2.20 Å R-free 0.229
1J4E FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE Deposited 2001-09-19	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Mutation：C72A, C239A, C289A, C338A Mutation：C72A, C239A, C289A, C338A Mutation：C72A, C239A, C289A, C338A Mutation：C72A, C239A, C289A, C338A	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.65 Å R-free 0.249
1ZAH Fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2005-04-06	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.80 Å R-free 0.205
1ZAI Fructose-1,6-bisphosphate Schiff base intermediate in FBP aldolase from rabbit muscle Deposited 2005-04-06	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Not recorded	2FP 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM) × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.76 Å R-free 0.190
1ZAJ Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with mannitol-1,6-bisphosphate, a competitive inhibitor Deposited 2005-04-06	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Not recorded	M2P D-MANNITOL-1,6-DIPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.89 Å R-free 0.204
1ZAL Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with partially disordered tagatose-1,6-bisphosphate, a weak competitive inhibitor Deposited 2005-04-06	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Not recorded	PO4 PHOSPHATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.89 Å R-free 0.211
2OT0 Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein Deposited 2007-02-07	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；HEPES, MgCl2, PEG 550 MME, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.05 Å R-free 0.200
2OT1 Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol AS-E phosphate, a competitive inhibitor Deposited 2007-02-07	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	N3P N-(4-CHLOROPHENYL)-3-(PHOSPHONOOXY)NAPHTHALENE-2-CARBOXAMIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.05 Å R-free 0.197
2QUT Dihydroxyacetone phosphate enamine intermediate in fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2007-08-06	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.88 Å R-free 0.191
2QUU Dihydroxyacetone phosphate Schiff base intermediate in mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2007-08-06	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：K146M Mutation：K146M Mutation：K146M Mutation：K146M	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.98 Å R-free 0.195
2QUV Phosphate ions in fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2007-08-06	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	PO4 PHOSPHATE ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.22 Å R-free 0.191
3B8D Fructose 1,6-bisphosphate aldolase from rabbit muscle Deposited 2007-11-01	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：E188Q Mutation：E188Q Mutation：E188Q Mutation：E188Q	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions SMALL TUBES；pH 7.4；293 K；40% ammonium sulphate 5mM EDTA, 100mM triethylamine, pH 7.4, SMALL TUBES, temperature 293K	Resolution 2.00 Å R-free 0.238
3BV4 Crystal structure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variant Deposited 2008-01-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 5–344（340 aa）	Mutation：D128V	SO4 SULFATE ION × 12 13P 1,3-DIHYDROXYACETONEPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.1；291 K；0.2 M ammonium sulfate, 25% PEG 2K monomethyl ether, 100 mM sodium acetate, pH 5.1, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.70 Å R-free 0.215
3DFN D33N mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2008-06-12	Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：D33N Mutation：D33N Mutation：D33N Mutation：D33N	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.86 Å R-free 0.188
3DFO Dihydroxyacetone phosphate Schiff base and enamine intermediates in D33N mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2008-06-12	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：D33N Mutation：D33N Mutation：D33N Mutation：D33N	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K, pH 7.50	Resolution 1.94 Å R-free 0.199
3DFP Phosphate ions in D33N mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2008-06-12	Different mutation/modification Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：D33N Mutation：D33N Mutation：D33N Mutation：D33N	PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.05 Å R-free 0.214
3DFQ D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2008-06-12	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：D33S Mutation：D33S Mutation：D33S Mutation：D33S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.82 Å R-free 0.188
3DFS Dihydroxyacetone phosphate Schiff base intermediate in D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle Deposited 2008-06-12	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：D33S Mutation：D33S Mutation：D33S Mutation：D33S	13P 1,3-DIHYDROXYACETONEPHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.03 Å R-free 0.187
3LGE Crystal structure of rabbit muscle aldolase-SNX9 LC4 complex Deposited 2010-01-20	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；PEG-MME 550, MgCl2, pH 7, Vapor Diffusion, Hanging drop, temperature 277K	Resolution 2.20 Å R-free 0.189
3TU9 Crystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphate Deposited 2011-09-16	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	5MM 2-O-methyl-1,6-di-O-phosphono-D-mannitol × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；17.5% PEG4000, 0.1 M HEPES sodium, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.09 Å R-free 0.201
5F4X Fructose-1,6-bisphosphate aldolase K229M mutant from rabbit muscle Deposited 2015-12-03	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Mutation：K229M Mutation：K229M Mutation：K229M Mutation：K229M	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；Sodium HEPES, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 1.84 Å R-free 0.174
5TLE Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-phosphate-naphthalene 6-bisphosphonate Deposited 2016-10-11	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	RD1 {[6-(phosphonooxy)naphthalen-2-yl]methylene}bis(phosphonic acid) × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；0.1M Sodium HEPES, 17.5% PEG 4000	Resolution 1.58 Å R-free 0.158
5TLH Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 2-naphthol 6-bisphosphonate Deposited 2016-10-11	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	RD2 [(6-hydroxynaphthalen-2-yl)methylene]bis(phosphonic acid) × 4 MDN METHYLENEDIPHOSPHONIC ACID × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；0.1M Sodium HEPES, 17.5% PEG 4000	Resolution 2.20 Å R-free 0.188
5TLW Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate Deposited 2016-10-12	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	RD3 {[4-(phosphonooxy)phenyl]methylene}bis(phosphonic acid) × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；0.1M Sodium HEPES, 17.5% PEG 4000	Resolution 2.29 Å R-free 0.191
5TLZ Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate Deposited 2016-10-12	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 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	N26 naphthalene-2,6-diyl bis[dihydrogen (phosphate)] × 4 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；296 K；0.1M Sodium HEPES, 17.5% PEG 4000	Resolution 1.97 Å R-free 0.166
5VY5 Rabbit muscle aldolase using 200keV Deposited 2017-05-24	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3 uL of sample/grid was manually blotted for 4 seconds prior to immediate plunge-freezing in liquid nitrogen-cooled ethane.	Resolution 2.60 Å
6ALD RABBIT MUSCLE ALDOLASE A/FRUCTOSE-1,6-BISPHOSPHATE COMPLEX Deposited 1998-12-23	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 1–363（363 aa） Chain B 1–363（363 aa） Chain C 1–363（363 aa） Chain D 1–363（363 aa）	Mutation：K146A Mutation：K146A Mutation：K146A Mutation：K146A	2FP 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM) × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.30 Å R-free 0.274
6MWQ Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP Deposited 2018-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 16–348（333 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Grids were frozen on a manual plunger at the Scripps Research Institute Core Microscopy Facility in a 4 degrees C cold room humidified to >95%.	Resolution 3.00 Å
6MWQ Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP Deposited 2018-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 16–348（333 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Grids were frozen on a manual plunger at the Scripps Research Institute Core Microscopy Facility in a 4 degrees C cold room humidified to >95%.	Resolution 3.00 Å
6MWQ Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP Deposited 2018-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 16–348（333 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Grids were frozen on a manual plunger at the Scripps Research Institute Core Microscopy Facility in a 4 degrees C cold room humidified to >95%.	Resolution 3.00 Å
6MWQ Single particle cryoEM structure of a DARPin-aldolase platform in complex with GFP Deposited 2018-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 16–348（333 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Grids were frozen on a manual plunger at the Scripps Research Institute Core Microscopy Facility in a 4 degrees C cold room humidified to >95%.	Resolution 3.00 Å
6V20 Rabbit muscle aldolase determined using single-particle cryo-EM at 200 keV Deposited 2019-11-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 3–345（343 aa） Chain B 3–345（343 aa） Chain C 3–345（343 aa） Chain D 3–345（343 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE；3 uL of sample/grid was manually blotted for 4 seconds prior to immediate plunge-freezing in liquid nitrogen-cooled ethane.	Resolution 2.13 Å
7K9L Aldolase, rabbit muscle (no beam-tilt refinement) Deposited 2020-09-29	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.90 Å
7K9X Aldolase, rabbit muscle (beam-tilt refinement x1) Deposited 2020-09-29	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
7KA2 Aldolase, rabbit muscle (beam-tilt refinement x2) Deposited 2020-09-29	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7KA3 Aldolase, rabbit muscle (beam-tilt refinement x3) Deposited 2020-09-29	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
7KA4 Aldolase, rabbit muscle (beam-tilt refinement x4) Deposited 2020-09-29	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
7VDC 3.28 A structure of the rabbit muscle aldolase Deposited 2021-09-06	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–364（364 aa） Chain B 1–364（364 aa） Chain C 1–364（364 aa） Chain D 1–364（364 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.28 Å
8EHG Rabbit muscle aldolase determined using single-particle cryo-EM with Apollo camera. Deposited 2022-09-14	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–364（364 aa） Chain B 1–364（364 aa） Chain C 1–364（364 aa） Chain D 1–364（364 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；DTT are added freshly before use. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.24 Å
8EW2 Cryo-EM structure of Aldolase embedded in crystalline ice Deposited 2022-10-21	Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–364（363 aa） Chain B 2–364（363 aa） Chain C 2–364（363 aa） Chain D 2–364（363 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；20 mM HEPES pH 7.5, 50-mM NaCl cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8TWK Cryo-EM structure of Aldolase collected by EPU on Glacios at 2.6 Angstrom resolution Deposited 2023-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–345（344 aa） Chain B 2–345（344 aa） Chain C 2–345（344 aa） Chain D 2–345（344 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8TWL Cryo-EM structure of Aldolase collected by SerialEM on Glacios at 2.7 Angstrom resolution Deposited 2023-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–345（344 aa） Chain B 2–345（344 aa） Chain C 2–345（344 aa） Chain D 2–345（344 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8TWM Cryo-EM structure of Aldolase collected by Leginon on Glacios at 2.6 Angstrom resolution Deposited 2023-08-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–345（344 aa） Chain B 2–345（344 aa） Chain C 2–345（344 aa） Chain D 2–345（344 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å

59 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ALDOA_RABIT
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–363； UniProt 2–364 Author chain B； PDBConstruct 1–363； UniProt 2–364 Author chain C； PDBConstruct 1–363； UniProt 2–364 Author chain D； PDBConstruct 1–363； UniProt 2–364

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3dft
Deposition date deposition_date	2008-06-12
Structure title title	Phosphate ions in D33S mutant fructose-1,6-bisphosphate aldolase from rabbit muscle
Keywords keywords	aldolase, mutant, phosphate, ion, Acetylation, Glycolysis, Lyase, Phosphoprotein, Schiff base; LYASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	35.31 Å
Radius of gyration Rg (electron density) rg_electron	34.50 Å
Forward intensity I(0) i0	365004000.00
Molecular weight molecular_weight	153320.0 kDa
Excluded volume excluded_volume	191540 Å³
Envelope volume envelope_volume	231360 Å³
Hydration-shell volume shell_volume	55062 Å³
Envelope diameter envelope_diameter	114.9 Å
Shell Rg shell_rg	41.98 Å
Envelope Rg envelope_rg	34.52 Å
Shape Rg shape_rg	34.51 Å
Total Rg total_rg	34.95 Å
Total atoms total_atoms	10774
Residues n_residues	1412
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	112.2 Å
Rg (real space) rg_real	35.17 Å
Rg uncertainty (real space) rg_real_error	0.68 Å
I(0) (real space) i0_real	3.6500e+08
I(0) uncertainty (real space) i0_real_error	5.8260e+06
Rg (reciprocal space) rg_reciprocal	35.26 Å
I(0) (reciprocal space) i0_reciprocal	365000000.0000
Solution quality estimate total_estimate	0.8970
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	42.4 Å
Skewness Skewness skewness	0.186
Kurtosis Kurtosis kurtosis	-0.492
Angular range angular_range	— – 0.2250 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	66330000.0000
Real-space data points n_real_points	46
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.900

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Fructose-bisphosphate aldolase A
Molecular weight formula_weight	39235.7 kDa
EC 编号 ec_number	4.1.2.13
Mutation mutation	D33S
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	12993

PHSHPALTPEQKKELSDIAHRIVAPGKGILAASESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY

来源 Source

来源生物 organism	Oryctolagus cuniculus
通用名 common_name	Rabbit
NCBI Class编号 ncbi_taxonomy_id	9986
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2219

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3dfta_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d3dftb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d3dftc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

Domain ID domain_id	d3dftd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.10 — Aldolase
Family Family family	c.1.10.1 — Class I aldolase

CATH v4.4 (4 domains)

Domain ID domain_id	3dftA00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3dftB00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3dftC00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

Domain ID domain_id	3dftD00
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	70 — Aldolase class I

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8. Citations (1)

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Unit-cell length a length_a	83.926 Å
Unit-cell length b length_b	103.615 Å
Unit-cell length c length_c	84.946 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.72 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	1.940 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	—
R_work r_work	0.1490
R_free r_free	0.2050

fit	/app/data/saxs_computation/df/3dft/3dft.fit
pddf	/app/data/pr_computation/df/3dft/3dft.pr.out
profile	/app/data/saxs_computation/df/3dft/3dft.dat