Current Protein Identity:P00361 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
1CER DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION Deposited 1995-11-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–331(331 aa)
Chain P 1–331(331 aa)
Chain Q 1–331(331 aa)
Chain R 1–331(331 aa)
Not recorded NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1CER DETERMINANTS OF ENZYME THERMOSTABILITY OBSERVED IN THE MOLECULAR STRUCTURE OF THERMUS AQUATICUS D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 2.5 ANGSTROMS RESOLUTION Deposited 1995-11-11 Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–331(331 aa)
Chain B 1–331(331 aa)
Chain C 1–331(331 aa)
Chain D 1–331(331 aa)
Not recorded NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
2G82 High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase: Role of 220's Loop Motion in Catalysis Deposited 2006-03-01 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain O 1–331(331 aa)
Chain P 1–331(331 aa)
Chain Q 1–331(331 aa)
Chain R 1–331(331 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 IPA ISOPROPYL ALCOHOL × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.3;295 K;23% PEG 300, 0.1 M Hepes, 15% isopropanol, and 5% glycerol, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 1.65 Å R-free 0.172
2G82 High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase: Role of 220's Loop Motion in Catalysis Deposited 2006-03-01 Assembly 2 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–331(331 aa)
Chain B 1–331(331 aa)
Chain C 1–331(331 aa)
Chain D 1–331(331 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 IPA ISOPROPYL ALCOHOL × 1 GOL GLYCEROL × 1 NA SODIUM ION × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.3;295 K;23% PEG 300, 0.1 M Hepes, 15% isopropanol, and 5% glycerol, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Resolution 1.65 Å R-free 0.172