1A72
| AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA) OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE ISOSTERIC NAD ANALOG CPAD | Descriptor: | 5-BETA-D-RIBOFURANOSYLPICOLINAMIDE ADENINE-DINUCLEOTIDE, HORSE LIVER ALCOHOL DEHYDROGENASE, ZINC ION | Authors: | Colby, T.D, Bahnson, B.J, Chin, J.K, Klinman, J.P, Goldstein, B.M. | Deposit date: | 1998-03-19 | Release date: | 1998-06-17 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes. Biochemistry, 37, 1998
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1A71
| TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND TRIFLUOROETHANOL | Descriptor: | LIVER ALCOHOL DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, TRIFLUOROETHANOL, ... | Authors: | Colby, T.D, Bahnson, B.J, Chin, J.K, Klinman, J.P, Goldstein, B.M. | Deposit date: | 1998-03-19 | Release date: | 1998-06-17 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes. Biochemistry, 37, 1998
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1B3O
| TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE | Descriptor: | 6-CHLOROPURINE RIBOSIDE, 5'-MONOPHOSPHATE, PROTEIN (INOSINE MONOPHOSPHATE DEHYDROGENASE 2), ... | Authors: | Colby, T.D, Vanderveen, K, Strickler, M.D, Goldstein, B.M. | Deposit date: | 1998-12-14 | Release date: | 1999-04-12 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc.Natl.Acad.Sci.USA, 96, 1999
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1AXE
| CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD AND INHIBITOR TRIFLUOROETHANOL | Descriptor: | ALCOHOL DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, TRIFLUOROETHANOL, ... | Authors: | Colby, T.D, Chin, J.K, Goldstein, B.M. | Deposit date: | 1997-10-15 | Release date: | 1998-04-15 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | A link between protein structure and enzyme catalyzed hydrogen tunneling. Proc.Natl.Acad.Sci.USA, 94, 1997
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1AXG
| CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION | Descriptor: | ALCOHOL DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, TRIFLUOROETHANOL, ... | Authors: | Colby, T.D, Chin, J.K, Bahnson, B.J, Goldstein, B.M, Klinman, J.P. | Deposit date: | 1997-10-15 | Release date: | 1998-04-15 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | A link between protein structure and enzyme catalyzed hydrogen tunneling. Proc.Natl.Acad.Sci.USA, 94, 1997
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6OWM
| Horse liver F93W alcohol dehydrogenase complexed with NAD and pentafluorobenzyl alcohol | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, 2,3,4,5,6-PENTAFLUOROBENZYL ALCOHOL, Alcohol dehydrogenase E chain, ... | Authors: | Plapp, B.V. | Deposit date: | 2019-05-10 | Release date: | 2019-05-22 | Last modified: | 2023-10-11 | Method: | X-RAY DIFFRACTION (1.1 Å) | Cite: | Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer. Biochemistry, 59, 2020
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6OWP
| Horse liver F93W alcohol dehydrogenase complexed with NAD and trifluoroethanol | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, Alcohol dehydrogenase E chain, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (ACIDIC FORM), ... | Authors: | Plapp, B.V. | Deposit date: | 2019-05-10 | Release date: | 2019-05-22 | Last modified: | 2023-10-11 | Method: | X-RAY DIFFRACTION (1.14 Å) | Cite: | Substitutions of Amino Acid Residues in the Substrate Binding Site of Horse Liver Alcohol Dehydrogenase Have Small Effects on the Structures but Significantly Affect Catalysis of Hydrogen Transfer. Biochemistry, 59, 2020
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