1TPB
 
 | | OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE | | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | | Deposit date: | 1994-02-03 | | Release date: | 1995-02-14 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | 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 | | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE | | Authors: | Zhang, Z, Sugio, S, Komives, E.A, Liu, K.D, Knowles, J.R, Petsko, G.A, Ringe, D. | | Deposit date: | 1994-02-03 | | Release date: | 1995-02-14 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | 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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3FZW
 | | Crystal Structure of Ketosteroid Isomerase D40N-D103N from Pseudomonas putida (pKSI) with bound equilenin | | Descriptor: | EQUILENIN, GLYCEROL, ISOPROPYL ALCOHOL, ... | | Authors: | Caaveiro, J.M.M, Ringe, D, Petsko, G.A. | | Deposit date: | 2009-01-26 | | Release date: | 2009-06-02 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (1.32 Å) | | Cite: | Hydrogen bond coupling in the ketosteroid isomerase active site.
Biochemistry, 48, 2009
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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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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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2DAB
 | | L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAL-5'-PHOSPHATE | | Descriptor: | D-AMINO ACID AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | | 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: | 2023-08-09 | | 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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2DAA
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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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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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6C4P
 | | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PMP Complex | | Descriptor: | 1,2-ETHANEDIOL, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, CALCIUM ION, ... | | Authors: | Kreinbring, C.A, Tu, Y, Liu, D, Berkowitz, D.B, Petsko, G.A, Ringe, D. | | Deposit date: | 2018-01-12 | | Release date: | 2018-04-25 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.
Biochemistry, 57, 2018
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6C2H
 | | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the Catalytic Core | | Descriptor: | 1,2-ETHANEDIOL, ACETATE ION, CALCIUM ION, ... | | Authors: | Kreinbring, C.A, Tu, Y, Liu, D, Petsko, G.A, Ringe, D. | | Deposit date: | 2018-01-08 | | Release date: | 2018-04-25 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (1.49 Å) | | Cite: | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.
Biochemistry, 57, 2018
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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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6C2Z
 | | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PLP-Aminoacrylate Intermediate | | Descriptor: | 1,2-ETHANEDIOL, 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID, CALCIUM ION, ... | | Authors: | Kreinbring, C.A, Tu, Y, Liu, D, Petsko, G.A, Ringe, D. | | Deposit date: | 2018-01-09 | | Release date: | 2018-04-25 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (1.37 Å) | | Cite: | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.
Biochemistry, 57, 2018
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6C2Q
 | | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: the Structure of the PLP-L-Serine Intermediate | | Descriptor: | 1,2-ETHANEDIOL, CALCIUM ION, CHLORIDE ION, ... | | Authors: | Kreinbring, C.A, Tu, Y, Liu, D, Petsko, G.A, Ringe, D. | | Deposit date: | 2018-01-08 | | Release date: | 2018-04-25 | | Last modified: | 2023-10-04 | | Method: | X-RAY DIFFRACTION (2.17 Å) | | Cite: | Crystal Structures of Cystathionine beta-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.
Biochemistry, 57, 2018
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1ELE
 | | STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS | | Descriptor: | CALCIUM ION, ELASTASE, N-(trifluoroacetyl)-L-valyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide, ... | | Authors: | Mattos, C, Petsko, G.A, Ringe, D. | | Deposit date: | 1994-10-24 | | Release date: | 1995-02-14 | | Last modified: | 2024-06-05 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.
Biochemistry, 34, 1995
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1ELD
 | | Structural analysis of the active site of porcine pancreatic elastase based on the x-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors | | Descriptor: | ACETIC ACID, CALCIUM ION, ELASTASE, ... | | Authors: | Mattos, C, Petsko, G.A, Ringe, D. | | Deposit date: | 1994-10-24 | | Release date: | 1995-02-14 | | Last modified: | 2024-06-05 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.
Biochemistry, 34, 1995
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5EAA
 | | ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION | | Descriptor: | ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE | | Authors: | Jeffery, C.J, Gloss, L.M, Petsko, G.A, Ringe, D. | | Deposit date: | 1998-12-29 | | Release date: | 2000-10-27 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2.4 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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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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4QYX
 | | Crystal structure of YDR533Cp | | Descriptor: | Probable chaperone protein HSP31 | | Authors: | Wilson, M.A, Amour, S.T, Collins, J.L, Ringe, D, Petsko, G.A. | | Deposit date: | 2014-07-26 | | Release date: | 2014-08-06 | | Last modified: | 2024-02-28 | | Method: | X-RAY DIFFRACTION (1.69 Å) | | Cite: | The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/PfpI superfamily.
Proc.Natl.Acad.Sci.USA, 101, 2004
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3GCH
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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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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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1ELF
 | | NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH | | Descriptor: | (TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO ETHYL-FORMAMIDE, CALCIUM ION, PORCINE PANCREATIC ELASTASE, ... | | Authors: | Ding, X, Rasmussen, B, Demuth, H.-U, Ringe, D, Steinmetz, A.C.U. | | Deposit date: | 1995-03-13 | | Release date: | 1995-07-10 | | Last modified: | 2024-06-05 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH.
Biochemistry, 34, 1995
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