Current Protein Identity:P56649 New Search
Main Difference Dimensions in This Set
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
1CRW CRYSTAL STRUCTURE OF APO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR AT 2.0A RESOLUTION Deposited 1999-08-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain G 1–333(333 aa)
Chain R 1–333(333 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6.1;291 K;pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 18K
Resolution 2.00 Å R-free 0.226
1DSS STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR Deposited 1997-06-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain G 1–333(333 aa) Fragment:NAD+ BINDING DOMAIN AND CATALYTIC DOMAIN
Chain R 1–333(333 aa) Fragment:NAD+ BINDING DOMAIN AND CATALYTIC DOMAIN
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1;290 K;THE PROTEIN SOLUTIONS CONTAINED 0.5MM NAD+, 1.0MM EDTA, 1.6M AMMONIUM SULFATE IN 0.1M PHOSPHATE BUFFER(PH 6.1) AND AN ENZYME CONCENTRATION OF 8MG/ML; THE SOLUTION IN RESERVOIR CONTAINED 2.7M AMMONIUM SULFATE IN SAME BUFFER, ROOM TEMPERATURE OF 17 DEGREES C., temperature 290K
Resolution 1.88 Å R-free 0.218
1IHX Crystal structure of two D-glyceraldehyde-3-phosphate dehydrogenase complexes: a case of asymmetry Deposited 2001-04-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–333(333 aa)
Chain B 1–333(333 aa)
Chain C 1–333(333 aa)
Chain D 1–333(333 aa)
Not recorded SO4 SULFATE ION × 8 SND THIONICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6.1;298 K;ammonium sulphate, pH 6.1, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.80 Å R-free 0.204
1IHY GAPDH complexed with ADP-ribose Deposited 2001-04-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–333(333 aa)
Chain B 1–333(333 aa)
Chain C 1–333(333 aa)
Chain D 1–333(333 aa)
Not recorded SO4 SULFATE ION × 8 APR ADENOSINE-5-DIPHOSPHORIBOSE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.1;298 K;ammonium sulphate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.00 Å R-free 0.207
1SZJ STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION Deposited 1997-02-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain G 1–333(333 aa) Fragment:NAD+ BINDING DOMAIN AND CATALYTIC DOMAIN
Chain R 1–333(333 aa) Fragment:NAD+ BINDING DOMAIN AND CATALYTIC DOMAIN
Not recorded SO4 SULFATE ION × 8 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.1;280 K;THE PROTEIN SOLUTIONS CONTAINED 0.5MM NAD+, 1.0MM EDTA, 1.6M AMMONIUM SULPHATE IN 0.1M PHOSPHATE BUFFER (PH 6.1) AND AN ENZYME CONCENTRATION OF 8MG/ML; THE SOLUTION IN RESERVOIR CONTAINED 2.7M AMMONIUM SULPHATE IN SAME BUFFER. THE CRYSTALLIZATION WAS CARRIED OUT AT 280K.
Resolution 2.00 Å R-free 0.223