4DM9
 
 | | The Crystal Structure of Ubiquitin Carboxy-terminal hydrolase L1 (UCHL1) bound to a tripeptide fluoromethyl ketone Z-VAE(OMe)-FMK | | Descriptor: | Tripeptide fluoromethyl ketone inhibitor Z-VAE(OMe)-FMK, Ubiquitin carboxyl-terminal hydrolase isozyme L1 | | Authors: | Davies, C.W, Chaney, J, Korbel, G, Ringe, D, Petsko, G.A, Ploegh, H, Das, C. | | Deposit date: | 2012-02-07 | | Release date: | 2012-05-23 | | Last modified: | 2023-09-13 | | Method: | X-RAY DIFFRACTION (2.35 Å) | | Cite: | The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK).
Bioorg.Med.Chem.Lett., 22, 2012
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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 | | Descriptor: | 2,3,4,N-TETRAHYDROXY-BUTYRIMIDIC ACID, MAGNESIUM ION, XYLOSE ISOMERASE | | Authors: | Allen, K.N, Lavie, A, Petsko, G.A, Ringe, D. | | Deposit date: | 1994-09-01 | | Release date: | 1995-07-10 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (1.6 Å) | | Cite: | 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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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: | 2024-05-22 | | 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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1ASG
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1ASE
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1ASC
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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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3AAT
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1ASF
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1ASD
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1ASB
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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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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: | 2024-06-05 | | 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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3DAA
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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: | 2024-06-05 | | 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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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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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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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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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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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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3GCH
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3VGN
 | | Crystal Structure of Ketosteroid Isomerase D40N from Pseudomonas putida (pKSI) with bound 3-fluoro-4-nitrophenol | | Descriptor: | 3-fluoro-4-nitrophenol, Steroid Delta-isomerase | | Authors: | Caaveiro, J.M.M, Pybus, B, Ringe, D, Petsko, G.A, Sigala, P.A. | | Deposit date: | 2011-08-16 | | Release date: | 2012-08-22 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.3 Å) | | Cite: | Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site
Proc.Natl.Acad.Sci.USA, 110, 2013
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4PST
 | | Multiconformer model for Escherichia coli dihydrofolate reductase at 277 K | | Descriptor: | Dihydrofolate reductase, FOLIC ACID, MANGANESE (II) ION, ... | | Authors: | Keedy, D.A, van den Bedem, H, Sivak, D.A, Petsko, G.A, Ringe, D, Wilson, M.A, Fraser, J.S. | | Deposit date: | 2014-03-07 | | Release date: | 2014-06-04 | | Last modified: | 2023-09-20 | | Method: | X-RAY DIFFRACTION (1.05 Å) | | Cite: | Crystal Cryocooling Distorts Conformational Heterogeneity in a Model Michaelis Complex of DHFR.
Structure, 22, 2014
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4PTJ
 | | Ensemble model for Escherichia coli dihydrofolate reductase at 277K | | Descriptor: | Dihydrofolate reductase, FOLIC ACID, MANGANESE (II) ION, ... | | Authors: | Keedy, D.A, van den Bedem, H, Sivak, D.A, Petsko, G.A, Ringe, D, Wilson, M.A, Fraser, J.S. | | Deposit date: | 2014-03-10 | | Release date: | 2014-05-14 | | Last modified: | 2023-09-20 | | Method: | X-RAY DIFFRACTION (1.05 Å) | | Cite: | Crystal Cryocooling Distorts Conformational Heterogeneity in a Model Michaelis Complex of DHFR.
Structure, 22, 2014
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4PSS
 | | Multiconformer model for Escherichia coli dihydrofolate reductase at 100K | | Descriptor: | Dihydrofolate reductase, FOLIC ACID, MANGANESE (II) ION, ... | | Authors: | Keedy, D.A, van den Bedem, H, Sivak, D.A, Petsko, G.A, Ringe, D, Wilson, M.A, Fraser, J.S. | | Deposit date: | 2014-03-07 | | Release date: | 2014-06-04 | | Last modified: | 2023-09-20 | | Method: | X-RAY DIFFRACTION (0.849 Å) | | Cite: | Crystal Cryocooling Distorts Conformational Heterogeneity in a Model Michaelis Complex of DHFR.
Structure, 22, 2014
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