Current Protein Identity:P35630 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
1Y9A Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate Deposited 2004-12-15 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–360(360 aa)
Chain C 1–360(360 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) Non-standard monomer:Yes (specific site not provided by mmCIF) ZN ZINC ION × 8 CAC CACODYLATE ION × 4 ACT ACETATE ION × 4 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;PEG 8000 14%w/v, 300 mM Mg Acetate, 200mM cacodylate at pH 6.5, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.81 Å R-free 0.177
2OUI D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica Deposited 2007-02-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–360(360 aa)
Chain B 1–360(360 aa)
Chain C 1–360(360 aa)
Chain D 1–360(360 aa)
Mutation:D275P Mutation:D275P Mutation:D275P Mutation:D275P ZN ZINC ION × 4 NO3 NITRATE ION × 4 CAC CACODYLATE ION × 4 EDO 1,2-ETHANEDIOL × 9 PGE TRIETHYLENE GLYCOL × 4 1PE PENTAETHYLENE GLYCOL × 1 CL CHLORIDE ION × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;8mg/mL protein, 25mM Tris-HCl, 50mM NaCl, 0.1mM DTT, 50mM ZnCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.77 Å R-free 0.178
3FPC Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH Deposited 2009-01-05 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 153–294(142 aa)
Chain B 153–294(142 aa)
Chain C 153–294(142 aa)
Chain D 153–294(142 aa)
Not recorded ZN ZINC ION × 4 CAC CACODYLATE ION × 4 OXY OXYGEN MOLECULE × 1 EDO 1,2-ETHANEDIOL × 14 NO3 NITRATE ION × 2 IMD IMIDAZOLE × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;8mg/mL protein [25mM Tris-HCl, 50mM NaCl, 0.1mM DTT, 50mM ZnCl2 (pH=7.5)] was mixed with 0.001 ml of reservoir solution [16% (w/v) PEG 8000, 200mM magnesium acetate tetrahydrate, 100mM Cacodylate buffer (pH 6.5)], vapor diffusion, hanging drop, temperature 298K
Resolution 1.40 Å R-free 0.155