Current Protein Identity:P04075 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification 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
1ALD ACTIVITY AND SPECIFICITY OF HUMAN ALDOLASES Deposited 1991-05-05 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–363(363 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
2ALD HUMAN MUSCLE ALDOLASE Deposited 1998-10-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–363(363 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;pH 7.5
Resolution 2.10 Å R-free 0.258
4ALD HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE Deposited 1998-07-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–363(363 aa)
Not recorded 2FP 1,6-FRUCTOSE DIPHOSPHATE (LINEAR FORM) × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;pH 7.5
Resolution 2.80 Å R-free 0.304
5KY6 Human muscle fructose-1,6-bisphosphate aldolase Deposited 2016-07-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
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;292 K;1.6M ammonium citrate tribasic
Resolution 1.94 Å R-free 0.223
6XMH Human aldolase A wild type Deposited 2020-06-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–364(364 aa)
Chain B 1–364(364 aa)
Not recorded PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.75;277 K;10% (w/v) PEG 8,000, 18% (v/v) glycerol, 0.04 M potassium phosphate, pH 5.75
Resolution 1.95 Å R-free 0.286
6XML Human aldolase A I98C Deposited 2020-06-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–364(364 aa)
Chain B 1–364(364 aa)
Mutation:I98C Mutation:I98C PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;10% (w/v) PEG 8000, 21% (v/v) glycerol in 0.04 M potassium phosphate, pH 6.0
Resolution 1.88 Å R-free 0.286
6XMM Human aldolase A I98S Deposited 2020-06-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–364(364 aa)
Chain B 1–364(364 aa)
Mutation:I98S Mutation:I98S PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;10% (w/v) PEG 8000, 15% (v/v) glycerol, 0.04 M potassium phosphate, pH 6.0
Resolution 2.11 Å R-free 0.295
6XMO Human aldolase A I98F Deposited 2020-06-30 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–364(364 aa)
Chain B 1–364(364 aa)
Mutation:I98F Mutation:I98F PO4 PHOSPHATE ION × 8 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.75;277 K;12% (w/v) PEG 8000, 15% (v/v) glycerol, 0.04 M potassium phosphate, pH 5.75
Resolution 2.60 Å R-free 0.259