5GCH
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1DAA
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1ASD
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1ASB
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1ASG
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1ASE
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7M7C
| Crystal Structure of Hip1 (Rv2224c) mutant - T466A/S228DHA (dehydroalanine) | Descriptor: | Carboxylesterase A | Authors: | Naffin-Olivos, J.L, Daab, A, Goldfarb, N.E, Doran, M.H, Baikovitz, J, Liu, D, Sun, S, White, A, Dunn, B.M, Rengarajan, J, Petsko, G.A, Ringe, D. | Deposit date: | 2021-03-27 | Release date: | 2022-03-30 | Last modified: | 2023-10-18 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Inhibitors and Inactivators of Mycobacterium tuberculosis serine protease Hip1 (Rv2224c) To Be Published
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1ASF
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1ASC
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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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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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7TIM
| STRUCTURE OF THE TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX: AN ANALOGUE OF THE INTERMEDIATE ON THE REACTION PATHWAY | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | Authors: | Davenport, R.C, Bash, P.A, Seaton, B.A, Karplus, M, Petsko, G.A, Ringe, D. | Deposit date: | 1991-04-23 | Release date: | 1993-10-31 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. Biochemistry, 30, 1991
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1G2W
| E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE | Descriptor: | ACETATE ION, D-ALANINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Lepore, B.W, Ringe, D. | Deposit date: | 2000-10-21 | Release date: | 2000-11-15 | Last modified: | 2021-11-03 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Studies on an Active Site Residue, E177, That Affects Binding of the Coenzyme in D-Amino Acid Transaminase, and Mechanistic Studies on a Suicide Substrate Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins, 10th Annual International Symposium on Vitamin B6, 2000
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1XYA
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | HYDROXIDE ION, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.81 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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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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1XYC
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.19 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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1XYB
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | Descriptor: | D-glucose, MAGNESIUM ION, XYLOSE ISOMERASE | Authors: | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | Deposit date: | 1994-01-03 | Release date: | 1994-05-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.96 Å) | Cite: | X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry, 33, 1994
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3LQS
| Complex Structure of D-Amino Acid Aminotransferase and 4-amino-4,5-dihydro-thiophenecarboxylic acid (ADTA) | Descriptor: | 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]THIOPHENE-2-CARBOXYLIC ACID, ACETIC ACID, D-alanine aminotransferase | Authors: | Lepore, B.W, Liu, D, Peng, Y, Fu, M, Yasuda, C, Manning, J.M, Silverman, R.B, Ringe, D. | Deposit date: | 2010-02-10 | Release date: | 2010-03-16 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Chiral discrimination among aminotransferases: inactivation by 4-amino-4,5-dihydrothiophenecarboxylic acid. Biochemistry, 49, 2010
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5DAA
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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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2SFP
| ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR | Descriptor: | PROPANOIC ACID, PROTEIN (ALANINE RACEMASE), PYRIDOXAL-5'-PHOSPHATE | Authors: | Morollo, A.A, Petsko, G.A, Ringe, D. | Deposit date: | 1999-02-16 | Release date: | 1999-02-24 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase. Biochemistry, 38, 1999
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6RHN
| HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT WITHOUT NUCLEOTIDE | Descriptor: | HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN | Authors: | Brenner, C, Garrison, P, Gilmour, J, Peisach, D, Ringe, D, Petsko, G.A, Lowenstein, J.M. | Deposit date: | 1997-02-27 | Release date: | 1997-06-16 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.15 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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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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