1NXB
| |
1BBG
| |
1B4X
| 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
| 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: | 2024-05-22 | 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
|
|
1BRM
| ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI | Descriptor: | ASPARTATE-SEMIALDEHYDE DEHYDROGENASE | Authors: | Hadfield, A.T, Kryger, G, Ouyang, J, Ringe, D, Petsko, G.A, Viola, R.E. | Deposit date: | 1998-08-24 | Release date: | 1999-06-22 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J.Mol.Biol., 289, 1999
|
|
1AZ1
| 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: | 2024-05-22 | 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
|
|
1BKH
| MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA | Descriptor: | MUCONATE LACTONIZING ENZYME | Authors: | Hasson, M.S, Schlichting, I, Moulai, J, Taylor, K, Barrett, W, Kenyon, G.L, Babbitt, P.C, Gerlt, J.A, Petsko, G.A, Ringe, D. | Deposit date: | 1998-07-07 | Release date: | 1998-10-21 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase. Proc.Natl.Acad.Sci.USA, 95, 1998
|
|
1MRA
| |
1TIM
| 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: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Atomic coordinates for triose phosphate isomerase from chicken muscle. Biochem.Biophys.Res.Commun., 72, 1976
|
|
1MDL
| |
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
|
|
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
|
|
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
|
|
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
|
|
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
|
|
1SBC
| |
1DTN
| |
1SOA
| Human DJ-1 with sulfinic acid | Descriptor: | RNA-binding protein regulatory subunit; oncogene DJ1 | Authors: | Canet-Aviles, R, Wilson, M.A, Miller, D.W, Ahmad, R, McLendon, C, Bandyopadhyay, S, Baptista, M.J, Ringe, D, Petsko, G.A, Cookson, M.R. | Deposit date: | 2004-03-13 | Release date: | 2004-06-22 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (1.2 Å) | Cite: | The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proc.Natl.Acad.Sci.USA, 101, 2004
|
|
1RKX
| Crystal Structure at 1.8 Angstrom of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis | Descriptor: | CDP-glucose-4,6-dehydratase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE | Authors: | Vogan, E.M, Bellamacina, C, He, X, Liu, H.W, Ringe, D, Petsko, G.A. | Deposit date: | 2003-11-23 | Release date: | 2004-03-30 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Crystal Structure at 1.8 A Resolution of CDP-d-Glucose 4,6-Dehydratase from Yersinia pseudotuberculosis Biochemistry, 43, 2004
|
|
1SFT
| ALANINE RACEMASE | Descriptor: | ACETATE ION, ALANINE RACEMASE, PYRIDOXAL-5'-PHOSPHATE | Authors: | Shaw, J.P, Petsko, G.A, Ringe, D. | Deposit date: | 1996-09-20 | Release date: | 1997-02-12 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry, 36, 1997
|
|
2ACU
| TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME | Descriptor: | ALDOSE REDUCTASE, CITRIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | Authors: | Bohren, K.M, Grimshaw, C.E, Lai, C.-J, Gabbay, K.H, Petsko, G.A, Harrison, D.H, Ringe, D. | Deposit date: | 1994-04-15 | Release date: | 1994-07-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.76 Å) | Cite: | Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry, 33, 1994
|
|
1MBC
| |
1ESB
| DIRECT STRUCTURE OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE | Descriptor: | CALCIUM ION, N-[(BENZYLOXY)CARBONYL]-L-ALANINE, PORCINE PANCREATIC ELASTASE, ... | Authors: | Ding, X, Rasmussen, B, Petsko, G.A, Ringe, D. | Deposit date: | 1994-02-04 | Release date: | 1994-04-30 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase. Biochemistry, 33, 1994
|
|
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
|
|
1GL3
| ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE IN COMPLEX WITH NADP AND SUBSTRATE ANALOGUE S-METHYL CYSTEINE SULFOXIDE | Descriptor: | ASPARTATE-SEMIALDEHYDE DEHYDROGENASE, CYSTEINE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE | Authors: | Hadfield, A.T, Kryger, G, Ouyang, J, Ringe, D, Petsko, G.A, Viola, R.E. | Deposit date: | 2001-08-23 | Release date: | 2001-11-01 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Active Site Analysis of the Potential Antimicrobial Target Aspartate Semialdehyde Dehydrogenase. Biochemistry, 40, 2001
|
|