1TPB
| OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE | 分子名称: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | 著者 | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | 登録日 | 1994-02-03 | 公開日 | 1995-02-14 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. Biochemistry, 34, 1995
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1TPC
| OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE | 分子名称: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | 著者 | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | 登録日 | 1994-02-03 | 公開日 | 1995-02-14 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules. Biochemistry, 34, 1995
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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 | 分子名称: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homocysteine, ... | 著者 | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | 登録日 | 2008-06-17 | 公開日 | 2008-07-29 | 最終更新日 | 2023-08-30 | 実験手法 | X-RAY DIFFRACTION (1.3 Å) | 主引用文献 | 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 | 分子名称: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ... | 著者 | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | 登録日 | 2008-06-17 | 公開日 | 2008-07-29 | 最終更新日 | 2023-08-30 | 実験手法 | X-RAY DIFFRACTION (0.95 Å) | 主引用文献 | 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 | 分子名称: | GLYCEROL, N-Acyl Homoserine Lactone Hydrolase, N-hexanoyl-L-homoserine, ... | 著者 | Liu, D, Momb, J, Thomas, P.W, Moulin, A, Petsko, G.A, Fast, W, Ringe, D. | 登録日 | 2008-06-17 | 公開日 | 2008-07-29 | 最終更新日 | 2023-08-30 | 実験手法 | X-RAY DIFFRACTION (1.4 Å) | 主引用文献 | Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry, 47, 2008
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5DAA
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2GYI
| DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A POTENT XYLOSE ISOMERASE INHIBITOR, D-THREONOHYDROXAMIC ACID, AND HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX | 分子名称: | 2,3,4,N-TETRAHYDROXY-BUTYRIMIDIC ACID, MAGNESIUM ION, XYLOSE ISOMERASE | 著者 | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | 登録日 | 1994-09-01 | 公開日 | 1995-07-10 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.6 Å) | 主引用文献 | Design, Synthesis, and Characterization of a Potent Xylose Isomerase Inhibitor, D-Threonohydroxamic Acid, and High-Resolution X-Ray Crystallographic Structure of the Enzyme-Inhibitor Complex Biochemistry, 34, 1995
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7GCH
| STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS | 分子名称: | 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 | 著者 | Brady, K, Ringe, D, Abeles, R.H. | 登録日 | 1990-04-06 | 公開日 | 1990-10-15 | 最終更新日 | 2011-07-13 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry, 29, 1990
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3FZW
| Crystal Structure of Ketosteroid Isomerase D40N-D103N from Pseudomonas putida (pKSI) with bound equilenin | 分子名称: | EQUILENIN, GLYCEROL, ISOPROPYL ALCOHOL, ... | 著者 | Caaveiro, J.M.M, Ringe, D, Petsko, G.A. | 登録日 | 2009-01-26 | 公開日 | 2009-06-02 | 最終更新日 | 2023-09-06 | 実験手法 | X-RAY DIFFRACTION (1.32 Å) | 主引用文献 | Hydrogen bond coupling in the ketosteroid isomerase active site. Biochemistry, 48, 2009
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5VWQ
| E.coli Aspartate aminotransferase-(1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP) | 分子名称: | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, Aspartate aminotransferase | 著者 | Mascarenhas, R, Lehrer, H, Liu, D, Ringe, D. | 登録日 | 2017-05-22 | 公開日 | 2017-08-30 | 最終更新日 | 2023-11-29 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover. Biochemistry, 56, 2017
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1B4X
| ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE | 分子名称: | ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE | 著者 | Jeffery, C.J, Gloss, L.M, Petsko, G.A, Ringe, D. | 登録日 | 1998-12-30 | 公開日 | 2000-10-27 | 最終更新日 | 2023-08-02 | 実験手法 | X-RAY DIFFRACTION (2.45 Å) | 主引用文献 | 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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2DAB
| L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE | 分子名称: | D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | 著者 | Sugio, S, Kashima, A, Kishimoto, K, Peisach, D, Petsko, G.A, Ringe, D, Yoshimura, T, Esaki, N. | 登録日 | 1997-11-30 | 公開日 | 1998-06-03 | 最終更新日 | 2023-08-09 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | 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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2INX
| Crystal Structure of Ketosteroid Isomerase D40N from Pseudomonas putida (pKSI) with bound 2,6-difluorophenol | 分子名称: | 2,6-DIFLUOROPHENOL, Steroid delta-isomerase | 著者 | Martinez Caaveiro, J.M, Pybus, B, Ringe, D, Petsko, G.A, Sigala, P, Kraut, D, Herschlag, D. | 登録日 | 2006-10-09 | 公開日 | 2007-10-23 | 最終更新日 | 2023-08-30 | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | 主引用文献 | Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. J.Am.Chem.Soc., 130, 2008
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1G2W
| E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE | 分子名称: | ACETATE ION, D-ALANINE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | 著者 | Lepore, B.W, Ringe, D. | 登録日 | 2000-10-21 | 公開日 | 2000-11-15 | 最終更新日 | 2021-11-03 | 実験手法 | X-RAY DIFFRACTION (2 Å) | 主引用文献 | 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 | 分子名称: | HYDROXIDE ION, MAGNESIUM ION, XYLOSE ISOMERASE | 著者 | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | 登録日 | 1994-01-03 | 公開日 | 1994-05-31 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.81 Å) | 主引用文献 | 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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1XYC
| X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS | 分子名称: | 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION, XYLOSE ISOMERASE | 著者 | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | 登録日 | 1994-01-03 | 公開日 | 1994-05-31 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (2.19 Å) | 主引用文献 | 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 | 分子名称: | D-glucose, MAGNESIUM ION, XYLOSE ISOMERASE | 著者 | Lavie, A, Allen, K.N, Petsko, G.A, Ringe, D. | 登録日 | 1994-01-03 | 公開日 | 1994-05-31 | 最終更新日 | 2024-02-14 | 実験手法 | X-RAY DIFFRACTION (1.96 Å) | 主引用文献 | 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) | 分子名称: | 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]THIOPHENE-2-CARBOXYLIC ACID, ACETIC ACID, D-alanine aminotransferase | 著者 | Lepore, B.W, Liu, D, Peng, Y, Fu, M, Yasuda, C, Manning, J.M, Silverman, R.B, Ringe, D. | 登録日 | 2010-02-10 | 公開日 | 2010-03-16 | 最終更新日 | 2024-02-21 | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | 主引用文献 | Chiral discrimination among aminotransferases: inactivation by 4-amino-4,5-dihydrothiophenecarboxylic acid. Biochemistry, 49, 2010
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7M7C
| Crystal Structure of Hip1 (Rv2224c) mutant - T466A/S228DHA (dehydroalanine) | 分子名称: | Carboxylesterase A | 著者 | 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. | 登録日 | 2021-03-27 | 公開日 | 2022-03-30 | 最終更新日 | 2023-10-18 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | Inhibitors and Inactivators of Mycobacterium tuberculosis serine protease Hip1 (Rv2224c) To Be Published
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2DAA
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1AZ1
| ALRESTATIN BOUND TO C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE | 分子名称: | ALDOSE REDUCTASE, ALRESTATIN, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | 著者 | Harrison, D.H.T, Bohren, K.M, Petsko, G.A, Ringe, D, Gabbay, K.H. | 登録日 | 1997-11-24 | 公開日 | 1998-03-18 | 最終更新日 | 2024-05-22 | 実験手法 | X-RAY DIFFRACTION (1.8 Å) | 主引用文献 | 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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6C2Z
| Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PLP-Aminoacrylate Intermediate | 分子名称: | 1,2-ETHANEDIOL, 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID, CALCIUM ION, ... | 著者 | Kreinbring, C.A, Tu, Y, Liu, D, Petsko, G.A, Ringe, D. | 登録日 | 2018-01-09 | 公開日 | 2018-04-25 | 最終更新日 | 2023-10-04 | 実験手法 | X-RAY DIFFRACTION (1.37 Å) | 主引用文献 | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time. Biochemistry, 57, 2018
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1AZ2
| CITRATE BOUND, C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE | 分子名称: | ALDOSE REDUCTASE, CITRIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | 著者 | Harrison, D.H, Bohren, K.M, Ringe, D, Petsko, G.A, Gabbay, K.H. | 登録日 | 1997-11-24 | 公開日 | 1998-03-18 | 最終更新日 | 2024-05-22 | 実験手法 | X-RAY DIFFRACTION (2.9 Å) | 主引用文献 | 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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6C2Q
| Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PLP-L-Serine Intermediate | 分子名称: | 1,2-ETHANEDIOL, CALCIUM ION, CHLORIDE ION, ... | 著者 | Kreinbring, C.A, Tu, Y, Liu, D, Petsko, G.A, Ringe, D. | 登録日 | 2018-01-08 | 公開日 | 2018-04-25 | 最終更新日 | 2023-10-04 | 実験手法 | X-RAY DIFFRACTION (2.17 Å) | 主引用文献 | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time. Biochemistry, 57, 2018
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6C4P
| Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PMP Complex | 分子名称: | 1,2-ETHANEDIOL, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, CALCIUM ION, ... | 著者 | Kreinbring, C.A, Tu, Y, Liu, D, Berkowitz, D.B, Petsko, G.A, Ringe, D. | 登録日 | 2018-01-12 | 公開日 | 2018-04-25 | 最終更新日 | 2023-10-04 | 実験手法 | X-RAY DIFFRACTION (2.3 Å) | 主引用文献 | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time. Biochemistry, 57, 2018
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