1BMA
| BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE | Descriptor: | (1R)-1-benzyl-1-methyl-1-(2-{[4-(1-methylethyl)phenyl]amino}-2-oxoethyl)-2-{(2S)-4-methyl-2-[(trifluoroacetyl)amino]pentanoyl}diazanium, CALCIUM ION, Chymotrypsin-like elastase family member 1, ... | Authors: | Peisach, E, Casebier, D, Gallion, S.L, Furth, P, Petsko, G.A, Hogan Jr, J.C, Ringe, D. | Deposit date: | 1995-05-01 | Release date: | 1995-12-07 | Last modified: | 2024-01-24 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Interaction of a peptidomimetic aminimide inhibitor with elastase. Science, 269, 1995
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1ASB
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1ASG
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1ASE
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1ASC
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1A0G
| L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE | Descriptor: | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, D-AMINO ACID AMINOTRANSFERASE | Authors: | Sugio, S, Kashima, A, Kishimoto, K, Peisach, D, Petsko, G.A, Ringe, D, Yoshimura, T, Esaki, N. | Deposit date: | 1997-11-30 | Release date: | 1998-06-03 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. Protein Eng., 11, 1998
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1ASA
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1BFD
| BENZOYLFORMATE DECARBOXYLASE FROM PSEUDOMONAS PUTIDA | Descriptor: | BENZOYLFORMATE DECARBOXYLASE, CALCIUM ION, MAGNESIUM ION, ... | Authors: | Hasson, M.S, Muscate, A, Mcleish, M.J, Polovnikova, L.S, Gerlt, J.A, Kenyon, G.L, Petsko, G.A, Ringe, D. | Deposit date: | 1998-04-30 | Release date: | 1998-06-24 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry, 37, 1998
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1BD0
| ALANINE RACEMASE COMPLEXED WITH ALANINE PHOSPHONATE | Descriptor: | ALANINE RACEMASE, {1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-PYRIDIN-4-YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC ACID | Authors: | Stamper, G.F, Morollo, A.A, Ringe, D. | Deposit date: | 1998-05-12 | Release date: | 1998-10-14 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine. Biochemistry, 37, 1998
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1AAW
| THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Almo, S.C, Smith, D.L, Danishefsky, A.T, Ringe, D. | Deposit date: | 1993-07-13 | Release date: | 1993-10-31 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng., 7, 1994
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1AAM
| THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION | Authors: | Almo, S.C, Smith, D.L, Danishefsky, A.T, Ringe, D. | Deposit date: | 1993-07-13 | Release date: | 1993-10-31 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. Protein Eng., 7, 1994
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1ASD
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1ASF
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1B4X
| ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE | Descriptor: | ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | Authors: | Jeffery, C.J, Gloss, L.M, Petsko, G.A, Ringe, D. | Deposit date: | 1998-12-30 | Release date: | 2000-10-27 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.45 Å) | Cite: | The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng., 13, 2000
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1AZ2
| CITRATE BOUND, C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE | Descriptor: | ALDOSE REDUCTASE, CITRIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | Authors: | Harrison, D.H, Bohren, K.M, Ringe, D, Petsko, G.A, Gabbay, K.H. | Deposit date: | 1997-11-24 | Release date: | 1998-03-18 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry, 36, 1997
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5GCH
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1AZ1
| ALRESTATIN BOUND TO C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE | Descriptor: | ALDOSE REDUCTASE, ALRESTATIN, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | Authors: | Harrison, D.H.T, Bohren, K.M, Petsko, G.A, Ringe, D, Gabbay, K.H. | Deposit date: | 1997-11-24 | Release date: | 1998-03-18 | Last modified: | 2023-08-02 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry, 36, 1997
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3DHC
| 1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homocysteine Bound to The catalytic Metal Center | Descriptor: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homocysteine, ... | Authors: | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | Deposit date: | 2008-06-17 | Release date: | 2008-07-29 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.3 Å) | Cite: | Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry, 47, 2008
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3DHA
| An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at An Alternative Site | Descriptor: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ... | Authors: | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | Deposit date: | 2008-06-17 | Release date: | 2008-07-29 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (0.95 Å) | Cite: | Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry, 47, 2008
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3DHB
| 1.4 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product N-Hexanoyl-L-Homoserine Bound at The Catalytic Metal Center | Descriptor: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ... | Authors: | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | Deposit date: | 2008-06-17 | Release date: | 2008-07-29 | Last modified: | 2023-08-30 | Method: | X-RAY DIFFRACTION (1.4 Å) | Cite: | Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry, 47, 2008
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5RHN
| HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP | Descriptor: | 8-BROMO-ADENOSINE-5'-MONOPHOSPHATE, HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN | Authors: | Brenner, C, Garrison, P, Gilmour, J, Peisach, D, Ringe, D, Petsko, G.A, Lowenstein, J.M. | Deposit date: | 1997-02-26 | Release date: | 1997-06-16 | Last modified: | 2024-03-06 | Method: | X-RAY DIFFRACTION (2.31 Å) | Cite: | Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat.Struct.Biol., 4, 1997
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4RHN
| HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH ADENOSINE | Descriptor: | HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN, alpha-D-ribofuranose | Authors: | Brenner, C, Garrison, P, Gilmour, J, Peisach, D, Ringe, D, Petsko, G.A, Lowenstein, J.M. | Deposit date: | 1997-02-26 | Release date: | 1997-06-16 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nat.Struct.Biol., 4, 1997
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1XYM
| THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID | Descriptor: | D-glucose, HYDROXIDE ION, MAGNESIUM ION, ... | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | Deposit date: | 1993-12-07 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry, 33, 1994
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1XYL
| THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID | Descriptor: | HYDROXIDE ION, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | Deposit date: | 1993-12-07 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid. Biochemistry, 33, 1994
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7GCH
| STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS | Descriptor: | 1,1,1-TRIFLUORO-3-((N-ACETYL)-L-LEUCYLAMIDO)-4-PHENYL-BUTAN-2-ONE(N-ACETYL-L-LEUCYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE), GAMMA-CHYMOTRYPSIN A | Authors: | Brady, K, Ringe, D, Abeles, R.H. | Deposit date: | 1990-04-06 | Release date: | 1990-10-15 | Last modified: | 2011-07-13 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry, 29, 1990
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