Current Protein Identity:P00362 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+ Deposited 1996-12-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9;pH 6.9
Resolution 2.50 Å R-free 0.214
1GD1 STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 1.8 ANGSTROMS RESOLUTION Deposited 1987-06-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Not recorded SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å
1NPT Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 replaced by Ala complexed with NAD+ Deposited 2003-01-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:C149A Mutation:C149A Mutation:C149A Mutation:C149A SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.18 Å R-free 0.210
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ Deposited 2003-01-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain Q 1–334(334 aa)
Mutation:C149S Mutation:C149S SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.11 Å R-free 0.249
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ Deposited 2003-01-21 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–334(334 aa)
Chain C 1–334(334 aa)
Mutation:C149S Mutation:C149S SO4 SULFATE ION × 2 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.11 Å R-free 0.249
1NQ5 Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ Deposited 2003-01-21 Assembly 3 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–334(334 aa)
Chain C 1–334(334 aa)
Mutation:C149S Mutation:C149S SO4 SULFATE ION × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.11 Å R-free 0.249
1NQA Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ala Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate Deposited 2003-01-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:C149A Mutation:C149A Mutation:C149A Mutation:C149A NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;PEG 4000, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.214
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate Deposited 2003-01-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain Q 1–334(334 aa)
Mutation:C149S Mutation:C149S NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.01 Å R-free 0.238
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate Deposited 2003-01-22 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–334(334 aa)
Chain C 1–334(334 aa)
Mutation:C149S Mutation:C149S NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.01 Å R-free 0.238
1NQO Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+ and D-Glyceraldehyde-3-Phosphate Deposited 2003-01-22 Assembly 3 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–334(334 aa)
Chain C 1–334(334 aa)
Mutation:C149S Mutation:C149S NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;PEG 4000, sodium acetate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.01 Å R-free 0.238
2DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH ASP 32 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+ Deposited 1996-12-19 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S Mutation:D32G, L187A, P188S SO4 SULFATE ION × 8 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9;pH 6.9
Resolution 2.20 Å R-free 0.265
2GD1 COENZYME-INDUCED CONFORMATIONAL CHANGES IN GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILLUS Deposited 1989-06-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Not recorded SO4 SULFATE ION × 8 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
3CMC Thioacylenzyme intermediate of Bacillus stearothermophilus phosphorylating GAPDH Deposited 2008-03-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 2–335(334 aa)
Chain P 2–335(334 aa)
Chain Q 2–335(334 aa)
Chain R 2–335(334 aa)
Not recorded SO4 SULFATE ION × 18 G3H GLYCERALDEHYDE-3-PHOSPHATE × 4 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 GOL GLYCEROL × 8 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.9;293 K;2.7 M Ammonium Sulfate, 100 mM Tris-HCl buffer pH 6.9, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.77 Å R-free 0.198
3DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NAD+ Deposited 1997-01-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9;pH 6.9
Resolution 2.45 Å R-free 0.275
4DBV GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE MUTANT WITH LEU 33 REPLACED BY THR, THR 34 REPLACED BY GLY, ASP 36 REPLACED BY GLY, LEU 187 REPLACED BY ALA, AND PRO 188 REPLACED BY SER COMPLEXED WITH NADP+ Deposited 1997-01-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–334(334 aa)
Chain P 1–334(334 aa)
Chain Q 1–334(334 aa)
Chain R 1–334(334 aa)
Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S Mutation:L33T, T34G, D36G, L187A, P188S SO4 SULFATE ION × 8 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.9;pH 6.9
Resolution 2.50 Å R-free 0.219