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2DEA
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CRYSTAL STRUCTURE OF THE AMINOPEPTIDASE OF AEROMONAS PROTEOLYTICA AT PH 4.7
Descriptor:Bacterial leucyl aminopeptidase, ZINC ION, SODIUM ION
Authors:Petsko, G.A., Ringe, D., Desmarais, W.
Deposit date:2006-02-10
Release date:2006-07-25
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.24 Å)
Cite:The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
J.Biol.Inorg.Chem., 11, 2006
3YPI
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ELECTROPHILIC CATALYSIS IN TRIOSEPHOSPHASE ISOMERASE: THE ROLE OF HISTIDINE-95
Descriptor:TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
Authors:Lolis, E., Petsko, G.A.
Deposit date:1990-12-31
Release date:1993-04-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
Biochemistry, 30, 1991
1NXB
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STRUCTURE AND FUNCTION OF SNAKE VENOM CURARIMIMETIC NEUROTOXINS
Descriptor:NEUROTOXIN B, SULFATE ION
Authors:Tsernoglou, D., Petsko, G.A.
Deposit date:1980-08-08
Release date:1981-01-27
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.38 Å)
Cite:Structure and function of snake venom curarimimetic neurotoxins.
Mol.Pharmacol., 14, 1978
1TPB
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OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Descriptor:TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
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:2011-07-13
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
1TPC
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OFFSET OF A CATALYTIC LESION BY A BOUND WATER SOLUBLE
Descriptor:TRIOSEPHOSPHATE ISOMERASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
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:2011-07-13
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
1YPI
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STRUCTURE OF YEAST TRIOSEPHOSPHATE ISOMERASE AT 1.9-ANGSTROMS RESOLUTION
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Alber, T., Lolis, E., Petsko, G.A.
Deposit date:1990-01-12
Release date:1991-01-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structure of yeast triosephosphate isomerase at 1.9-A resolution.
Biochemistry, 29, 1990
2YPI
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CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-ANGSTROMS RESOLUTION. IMPLICATIONS FOR CATALYSIS
Descriptor:TRIOSEPHOSPHATE ISOMERASE, 2-PHOSPHOGLYCOLIC ACID
Authors:Lolis, E., Petsko, G.A.
Deposit date:1990-01-12
Release date:1991-01-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
Biochemistry, 29, 1990
1TIM
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STRUCTURE OF TRIOSE PHOSPHATE ISOMERASE FROM CHICKEN MUSCLE
Descriptor:TRIOSEPHOSPHATE ISOMERASE
Authors:Banner, D.W., Bloomer, A.C., Petsko, G.A., Phillips, D.C., Wilson, I.A.
Deposit date:1976-09-01
Release date:1976-10-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Atomic coordinates for triose phosphate isomerase from chicken muscle.
Biochem.Biophys.Res.Commun., 72, 1976
2GYI
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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:XYLOSE ISOMERASE, MAGNESIUM ION, 2,3,4,N-TETRAHYDROXY-BUTYRIMIDIC ACID
Authors:Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D.
Deposit date:1994-09-01
Release date:1995-07-10
Last modified:2017-11-29
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
1DTN
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MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE
Descriptor:MANDELATE RACEMASE, MAGNESIUM ION, ATROLACTIC ACID (2-PHENYL-LACTIC ACID)
Authors:Clifton, J.G., Petsko, G.A.
Deposit date:1996-03-28
Release date:1996-10-14
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.
Biochemistry, 34, 1995
1MDL
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MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE
Descriptor:MANDELATE RACEMASE, MAGNESIUM ION, (R)-MANDELIC ACID, ...
Authors:Clifton, J.G., Petsko, G.A.
Deposit date:1996-03-29
Release date:1996-10-14
Last modified:2018-03-14
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.
Biochemistry, 34, 1995
1MRA
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MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE
Descriptor:MANDELATE RACEMASE, MAGNESIUM ION, ATROLACTIC ACID (2-PHENYL-LACTIC ACID)
Authors:Clifton, J.G., Petsko, G.A.
Deposit date:1996-03-12
Release date:1996-08-01
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.
Biochemistry, 35, 1996
1XYA
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, MAGNESIUM ION, HYDROXIDE ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
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
1XYB
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, D-GLUCOSE IN LINEAR FORM, MAGNESIUM ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
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
1XYC
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X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS
Descriptor:XYLOSE ISOMERASE, 3-O-METHYLFRUCTOSE IN LINEAR FORM, MAGNESIUM ION
Authors:Lavie, A., Allen, K.N., Petsko, G.A., Ringe, D.
Deposit date:1994-01-03
Release date:1994-05-31
Last modified:2017-11-29
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
1XYL
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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:XYLOSE ISOMERASE, MAGNESIUM ION, HYDROXIDE ION
Authors:Allen, K.N., Lavie, A., Petsko, G.A., Ringe, D.
Deposit date:1993-12-07
Release date:1994-05-31
Last modified:2017-11-29
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
1XYM
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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:XYLOSE ISOMERASE, D-GLUCOSE IN LINEAR FORM, 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:2017-11-29
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
2SFP
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ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR
Descriptor:PROTEIN (ALANINE RACEMASE), PYRIDOXAL-5'-PHOSPHATE, PROPANOIC ACID
Authors:Morollo, A.A., Petsko, G.A., Ringe, D.
Deposit date:1999-02-16
Release date:1999-02-24
Last modified:2011-07-13
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
3FZW
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CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE D40N-D103N FROM PSEUDOMONAS PUTIDA (PKSI) WITH BOUND EQUILENIN
Descriptor:Steroid Delta-isomerase, EQUILENIN, GLYCEROL, ...
Authors:Caaveiro, J.M.M., Ringe, D., Petsko, G.A.
Deposit date:2009-01-26
Release date:2009-06-02
Last modified:2017-11-01
Method:X-RAY DIFFRACTION (1.32 Å)
Cite:Hydrogen bond coupling in the ketosteroid isomerase active site.
Biochemistry, 48, 2009
6FAB
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THREE-DIMENSIONAL STRUCTURE OF MURINE ANTI-P-AZOPHENYLARSONATE FAB 36-71. 1. X-RAY CRYSTALLOGRAPHY, SITE-DIRECTED MUTAGENESIS, AND MODELING OF THE COMPLEX WITH HAPTEN
Descriptor:IGG1-KAPPA 36-71 FAB (LIGHT CHAIN), IGG1-KAPPA 36-71 FAB (HEAVY CHAIN)
Authors:Strong, R.K., Rose, D.R., Petsko, G.A., Sharon, J., Margolies, M.N.
Deposit date:1991-01-17
Release date:1993-01-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten.
Biochemistry, 30, 1991
1A0G
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L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE
Descriptor:D-AMINO ACID AMINOTRANSFERASE, 4'-DEOXY-4'-AMINOPYRIDOXAL-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:2011-07-13
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
1BFD
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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:2011-11-16
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
1BMA
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BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE
Descriptor:Chymotrypsin-like elastase family member 1, CALCIUM ION, SULFATE ION, ...
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:2012-12-12
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Interaction of a peptidomimetic aminimide inhibitor with elastase.
Science, 269, 1995
1ELD
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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:ELASTASE, N-(trifluoroacetyl)-L-phenylalanyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide, CALCIUM ION, ...
Authors:Mattos, C., Petsko, G.A., Ringe, D.
Deposit date:1994-10-24
Release date:1995-02-14
Last modified:2012-12-12
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
1ELE
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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:ELASTASE, N-(trifluoroacetyl)-L-valyl-N-[4-(trifluoromethyl)phenyl]-L-alaninamide, CALCIUM ION, ...
Authors:Mattos, C., Petsko, G.A., Ringe, D.
Deposit date:1994-10-24
Release date:1995-02-14
Last modified:2012-12-12
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