1DAA
 
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1DDN
 | | DIPHTHERIA TOX REPRESSOR (C102D MUTANT)/TOX DNA OPERATOR COMPLEX | | Descriptor: | 33 BASE DNA CONTAINING TOXIN OPERATOR, DIPHTHERIA TOX REPRESSOR, NICKEL (II) ION | | Authors: | White, A, Ding, X, Vanderspek, J.C, Murphy, J.R, Ringe, D. | | Deposit date: | 1998-06-23 | | Release date: | 1998-10-14 | | Last modified: | 2023-08-02 | | Method: | X-RAY DIFFRACTION (3 Å) | | Cite: | Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex.
Nature, 394, 1998
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1CP6
 | | 1-BUTANEBORONIC ACID BINDING TO AEROMONAS PROTEOLYTICA AMINOPEPTIDASE | | Descriptor: | 1-BUTANE BORONIC ACID, PROTEIN (AMINOPEPTIDASE), ZINC ION | | Authors: | Depaola, C.C, Bennett, B, Holz, R.C, Ringe, D, Petsko, G.A. | | Deposit date: | 1999-06-08 | | Release date: | 1999-06-17 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development.
Biochemistry, 38, 1999
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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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1BKH
 | | MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA | | Descriptor: | MUCONATE LACTONIZING ENZYME | | Authors: | Hasson, M.S, Schlichting, I, Moulai, J, Taylor, K, Barrett, W, Kenyon, G.L, Babbitt, P.C, Gerlt, J.A, Petsko, G.A, Ringe, D. | | Deposit date: | 1998-07-07 | | Release date: | 1998-10-21 | | Last modified: | 2023-08-02 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.
Proc.Natl.Acad.Sci.USA, 95, 1998
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1BRM
 | | ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI | | Descriptor: | ASPARTATE-SEMIALDEHYDE DEHYDROGENASE | | Authors: | Hadfield, A.T, Kryger, G, Ouyang, J, Ringe, D, Petsko, G.A, Viola, R.E. | | Deposit date: | 1998-08-24 | | Release date: | 1999-06-22 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.
J.Mol.Biol., 289, 1999
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1CM7
 | | 3-ISOPROPYLMALATE DEHYDROGENASE FROM ESCHERICHIA COLI | | Descriptor: | PROTEIN (3-ISOPROPYLMALATE DEHYDROGENASE) | | Authors: | Wallon, G, Kryger, G, Lovett, S.T, Oshima, T, Ringe, D, Petsko, G.A. | | Deposit date: | 1999-05-17 | | Release date: | 1999-07-01 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (2.06 Å) | | Cite: | Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.
J.Mol.Biol., 266, 1997
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1CNZ
 | | 3-ISOPROPYLMALATE DEHYDROGENASE (IPMDH) FROM SALMONELLA TYPHIMURIUM | | Descriptor: | MANGANESE (II) ION, PROTEIN (3-ISOPROPYLMALATE DEHYDROGENASE), SULFATE ION | | Authors: | Wallon, G, Kryger, G, Lovett, S.T, Oshima, T, Ringe, D, Petsko, G.A. | | Deposit date: | 1999-05-24 | | Release date: | 1999-06-01 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (1.76 Å) | | Cite: | Crystal Structures of Eschericia Coli and Salmonella Typhimurium 3-
Isopropylmalate Dehydrogenase and Comparison with Their Thermophilic
Counterpart from Thermus Thermophilus
J.Mol.Biol., 266, 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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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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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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1ASG
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1ASB
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1ASE
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1ASC
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5GCH
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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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5DAA
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6GCH
 | | STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS | | Descriptor: | 1,1,1-TRIFLUORO-3-ACETAMIDO-4-PHENYL BUTAN-2-ONE(N-ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE), GAMMA-CHYMOTRYPSIN A | | Authors: | Brady, K, Wei, A, Ringe, D, Abeles, R.H. | | Deposit date: | 1990-04-06 | | Release date: | 1990-10-15 | | Last modified: | 2011-07-13 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors.
Biochemistry, 29, 1990
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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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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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