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THE STRUCTURE OF LOBSTER APO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 3.0 ANGSTROMS RESOLUTION[OXIDOREDUCTASE(ALDEHYDE(D)-NAD(A))]
View in iCn3D Similar StructuresProteinsConserved Domains
Crystal Structure of Human Liver GAPDH[OXIDOREDUCTASE]
View in iCn3D Similar StructuresProteinsConserved DomainsPubChem Compound
CRYSTAL STRUCTURE OF APO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR AT 2.0A RESOLUTION[OXIDOREDUCTASE]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION[OXIDOREDUCTASE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
GAPDH complexed with ADP-ribose[OXIDOREDUCTASE]
Crystal structure of two D-glyceraldehyde-3-phosphate dehydrogenase complexes: a case of asymmetry[OXIDOREDUCTASE]
STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR[ACTIVE-SITE CARBOXYMETHYLATION]
Crystal structure of the rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH)[OXIDOREDUCTASE]
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Crystal Structure Of Human Placental Glyceraldehyde-3-Phosphate Dehydrogenase At 1.75 Resolution[OXIDOREDUCTASE]
TWINNING IN CRYSTALS OF HUMAN SKELETAL MUSCLE D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE[OXIDOREDUCTASE (NAD(A)-ALDEHYDE(D))]
Crystal structure of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) complex with NAD and phosphate[OXIDOREDUCTASE]
Crystal structure of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) complex with NAD, a binary form[OXIDOREDUCTASE]
Crystal structure and Functional Analysis of Glyceraldehyde-3-phosphate Dehydrogenase from Oryza Sativa[OXIDOREDUCTASE]
View in iCn3D Similar StructuresProteinsPubChem Compound
Crystal structure of MES buffer bound form of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli[STRUCTURAL GENOMICS, OXIDOREDUCTASE]
STRUCTURAL ANALYSIS OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE FROM ESCHERICHIA COLI: DIRECT EVIDENCE FOR SUBSTRATE BINDING AND COFACTOR-INDUCED CONFORMATIONAL CHANGES[OXIDOREDUCTASE]
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