Current Protein Identity:P25984 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
1JQB Alcohol Dehydrogenase from Clostridium Beijerinckii: Crystal Structure of Mutant with Enhanced Thermal Stability Deposited 2001-08-05 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–351(351 aa)
Chain B 1–351(351 aa)
Chain C 1–351(351 aa)
Chain D 1–351(351 aa)
Mutation:Q165E,M304R,V224E,S254K Mutation:Q165E,M304R,V224E,S254K Mutation:Q165E,M304R,V224E,S254K Mutation:Q165E,M304R,V224E,S254K ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8.2;292 K;PEG 4000, Tris-Cl, NaCl, NADP, ZnCl2, pH 8.2, VAPOR DIFFUSION, HANGING DROP, temperature 292.0K
Resolution 1.97 Å R-free 0.247
1KEV STRUCTURE OF NADP-DEPENDENT ALCOHOL DEHYDROGENASE Deposited 1996-10-21 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–351(351 aa)
Chain B 1–351(351 aa)
Chain C 1–351(351 aa)
Chain D 1–351(351 aa)
Not recorded ZN ZINC ION × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.2;SEE REFERENCE 1, pH 8.2
Resolution 2.05 Å R-free 0.259
1PED BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM) Deposited 1995-12-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–351(351 aa)
Chain B 1–351(351 aa)
Chain C 1–351(351 aa)
Chain D 1–351(351 aa)
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;SEE REFERENCE 1., pH 7.5
Resolution 2.15 Å R-free 0.258
2B83 A single amino acid substitution in the Clostridium beijerinckii alcohol dehydrogenase is critical for thermostabilization Deposited 2005-10-06 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–351(351 aa)
Chain B 1–351(351 aa)
Chain C 1–351(351 aa)
Chain D 1–351(351 aa)
Mutation:Q100P Mutation:Q100P Mutation:Q100P Mutation:Q100P ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH;pH 6;298 K;5% PEG 100; 30% PEG600; 10% Glycerol; MES 0.1M, Microbatch, temperature 298K
Resolution 2.25 Å R-free 0.230
3FPL Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH Deposited 2009-01-05 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–152(152 aa)
Chain A 296–351(56 aa)
Not recorded ZN ZINC ION × 4 CL CHLORIDE ION × 8 EDO 1,2-ETHANEDIOL × 4 CAC CACODYLATE ION × 4 PGE TRIETHYLENE GLYCOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6;298 K;Single crystals of apo-22(CTC) were obtained by the microbatch method under oil at 18 C, using the IMPAX 1-5 robot. The apo-22(CTC) (10mg/mL) was crystallized in a mixture containing 100mM ammonium acetate, 15% (w/v) PEG 4000, 25mM NaCl, 50mM DTT, 25mM ZnCl2 and 50mM tri-citrate dihydrate (pH sodium 5.6), Microbatch, temperature 298K
Resolution 1.90 Å R-free 0.172
3FSR Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH Deposited 2009-01-11 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 153–295(143 aa)
Chain B 153–295(143 aa)
Chain C 153–295(143 aa)
Chain D 153–295(143 aa)
Not recorded ZN ZINC ION × 6 EDO 1,2-ETHANEDIOL × 5 CL CHLORIDE ION × 1 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 0.001ml 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 2.20 Å R-free 0.220
3FTN Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH Deposited 2009-01-13 Assembly 1 Insufficient information Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 153–295(143 aa)
Chain B 153–295(143 aa)
Chain C 153–295(143 aa)
Chain D 153–295(143 aa)
Mutation:Q165E, S254K Mutation:Q165E, S254K Mutation:Q165E, S254K Mutation:Q165E, S254K ZN ZINC ION × 4 ACT ACETATE ION × 4 EDO 1,2-ETHANEDIOL × 11 CL CHLORIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;8 mg/mL protein, 25 mM Tris-HCl, 50 mM NaCl, 0.1 mM DTT, 50 mM ZnCl2 (pH=7.5)] was mixed with 1 microliter of reservoir solution [16% (w/v) PEG8K, 200 mM magnesium acetate tetrahydrate, 100 mM Cacodylate buffer (pH 6.5), vapor diffusion, hanging drop, temperature 298K
Resolution 2.19 Å R-free 0.228
6SCH NADH-dependent variant of CBADH Deposited 2019-07-24 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 1–351(351 aa)
Chain B 1–351(351 aa)
Chain C 1–351(351 aa)
Chain D 1–351(351 aa)
Not recorded NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 4 2PE NONAETHYLENE GLYCOL × 8 ZN ZINC ION × 4 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;290 K;900 mM sodium citrate, 100 mM imidazole pH 8
Resolution 2.20 Å R-free 0.208