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1BMA
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BU of 1bma by Molmil
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
1A0G
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BU of 1a0g by Molmil
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:2023-08-02
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
1ASA
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BU of 1asa by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASB
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BU of 1asb by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.6 Å)
Cite:The Structural Basis for the Reduced Activity of the D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASG
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BU of 1asg by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1ASE
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BU of 1ase by Molmil
THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH PLP-N-OXIDE
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE-N-OXIDE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with Plp-N-Oxide
To be Published
1ASC
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BU of 1asc by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE D223A(D222A) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor: ASPARTATE AMINOTRANSFERASE, N-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The Structural Basis for the Reduced Activity of the D223A(D222A) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1AAW
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BU of 1aaw by Molmil
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
1AAM
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BU of 1aam by Molmil
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
1ASD
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BU of 1asd by Molmil
THE STRUCTURE OF WILD TYPE E. COLI ASPARTATE AMINOTRANSFERASE RECONSTITUTED WITH N-MEPLP
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, N-METHYL-PYRIDOXAL-5'-PHOSPHATE
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:The Structure of Wild Type E. Coli Aspartate Aminotransferase Reconstituted with N-Meplp
To be Published
1ASF
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BU of 1asf by Molmil
THE STRUCTURAL BASIS FOR THE REDUCED ACTIVITY OF THE Y226F(Y225F) ACTIVE SITE MUTANT OF E. COLI ASPARTATE AMINOTRANSFERASE
Descriptor: ASPARTATE AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, SULFATE ION
Authors:Schumacher, C, Ringe, D.
Deposit date:1993-08-27
Release date:1994-04-30
Last modified:2012-07-25
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The Structural Basis for the Reduced Activity of the Y226F(Y225F) Active Site Mutant of E. Coli Aspartate Aminotransferase
To be Published
1BFD
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BU of 1bfd by Molmil
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
1BD0
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BU of 1bd0 by Molmil
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
1B4X
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BU of 1b4x by Molmil
ASPARTATE AMINOTRANSFERASE FROM E. COLI, C191S MUTATION, WITH BOUND MALEATE
Descriptor: ASPARTATE AMINOTRANSFERASE, MALEIC ACID, PYRIDOXAL-5'-PHOSPHATE
Authors:Jeffery, C.J, Gloss, L.M, Petsko, G.A, Ringe, D.
Deposit date:1998-12-30
Release date:2000-10-27
Last modified:2023-08-02
Method:X-RAY DIFFRACTION (2.45 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
1AZ2
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BU of 1az2 by Molmil
CITRATE BOUND, C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE
Descriptor: ALDOSE REDUCTASE, CITRIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Authors:Harrison, D.H, Bohren, K.M, Ringe, D, Petsko, G.A, Gabbay, K.H.
Deposit date:1997-11-24
Release date:1998-03-18
Last modified:2023-08-02
Method:X-RAY DIFFRACTION (2.9 Å)
Cite:The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
Biochemistry, 36, 1997
1AZ1
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BU of 1az1 by Molmil
ALRESTATIN BOUND TO C298A/W219Y MUTANT HUMAN ALDOSE REDUCTASE
Descriptor: ALDOSE REDUCTASE, ALRESTATIN, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Authors:Harrison, D.H.T, Bohren, K.M, Petsko, G.A, Ringe, D, Gabbay, K.H.
Deposit date:1997-11-24
Release date:1998-03-18
Last modified:2023-08-02
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.
Biochemistry, 36, 1997
6GCH
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BU of 6gch by Molmil
STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS
Descriptor: 1,1,1-TRIFLUORO-3-ACETAMIDO-4-PHENYL BUTAN-2-ONE(N-ACETYL-L-PHENYLALANYL TRIFLUOROMETHYL KETONE), GAMMA-CHYMOTRYPSIN A
Authors:Brady, K, Wei, A, Ringe, D, Abeles, R.H.
Deposit date:1990-04-06
Release date:1990-10-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors.
Biochemistry, 29, 1990
5RHN
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BU of 5rhn by Molmil
HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT COMPLEXED WITH 8-BR-AMP
Descriptor: 8-BROMO-ADENOSINE-5'-MONOPHOSPHATE, HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN
Authors:Brenner, C, Garrison, P, Gilmour, J, Peisach, D, Ringe, D, Petsko, G.A, Lowenstein, J.M.
Deposit date:1997-02-26
Release date:1997-06-16
Last modified:2024-03-06
Method:X-RAY DIFFRACTION (2.31 Å)
Cite:Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
Nat.Struct.Biol., 4, 1997
4RHN
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BU of 4rhn by Molmil
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
3DHC
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BU of 3dhc by Molmil
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
3DHA
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BU of 3dha by Molmil
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
3DHB
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BU of 3dhb by Molmil
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
1XYM
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BU of 1xym by Molmil
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
1XYL
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BU of 1xyl by Molmil
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
5GCH
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BU of 5gch by Molmil
CHEMISTRY OF CAGED ENZYMES /II$. PHOTOACTIVATION OF INHIBITED CHYMOTRYPSIN
Descriptor: GAMMA-CHYMOTRYPSIN A
Authors:Stoddard, B.L, Ringe, D, Petsko, G.A.
Deposit date:1989-09-25
Release date:1990-10-15
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.7 Å)
Cite:Photolysis and deacylation of inhibited chymotrypsin.
Biochemistry, 29, 1990

217705

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