4MDH
| |
1C80
| REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE | Descriptor: | FRUCTOSE-2,6-BISPHOSPHATASE, GUANOSINE-5'-TRIPHOSPHATE, PHOSPHATE ION | Authors: | Lee, Y.H, Olson, T.W, McClard, R.W, Witte, J.F, McFarlan, S.C, Banaszak, L.J, Levitt, D.G, Lange, A.J. | Deposit date: | 2000-04-03 | Release date: | 2003-06-10 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Reaction Mechanism of Fructose-2,6-bisphosphatase Suggested by the Crystal Structures of a pseudo-Michaelis complex and Metabolite Complexes To be Published
|
|
1C7Z
| REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE | Descriptor: | FRUCTOSE-2,6-BISPHOSPHATASE, GLYCERALDEHYDE-3-PHOSPHATE, PHOSPHATE ION | Authors: | Lee, Y.H, Olson, T.W, McClard, R.W, Witte, J.F, McFarlan, S.C, Banaszak, L.J, Levitt, D.G, Lange, A.J. | Deposit date: | 2000-04-03 | Release date: | 2003-06-10 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Reaction Mechanism of Fructose-2,6-bisphosphatase Suggested by the Crystal Structures of a pseudo-Michaelis complex and Metabolite Complexes To be Published
|
|
1SC6
| |
1C81
| MICHAELIS COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol, FRUCTOSE-2,6-BISPHOSPHATASE | Authors: | Lee, Y.H, Olson, T.W, McClard, R.W, Witte, J.F, McFarlan, S.C, Banaszak, L.J, Levitt, D.G, Lange, A.J. | Deposit date: | 2000-04-03 | Release date: | 2003-06-10 | Last modified: | 2024-03-13 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Reaction Mechanism of Fructose-2,6-bisphosphatase Suggested by the Crystal Structures of a pseudo-Michaelis complex and Metabolite Complexes To be Published
|
|
1SEV
| Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures | Descriptor: | Malate dehydrogenase, glyoxysomal precursor | Authors: | Cox, B.R, Chit, M.M, Weaver, T.M, Bailey, J, Gietl, C, Bell, E, Banaszak, L.J. | Deposit date: | 2004-02-18 | Release date: | 2005-01-25 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.55 Å) | Cite: | Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence Febs J., 272, 2005
|
|
1IFB
| |
1IE3
| CRYSTAL STRUCTURE OF R153C E. COLI MALATE DEHYDROGENASE | Descriptor: | MALATE DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PYRUVIC ACID | Authors: | Bell, J.K, Yennawar, H.P, Wright, S.K, Thompson, J.R, Viola, R.E, Banaszak, L.J. | Deposit date: | 2001-04-05 | Release date: | 2001-09-19 | Last modified: | 2023-11-15 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Structural Analyses of a Malate Dehydrogenase with a Variable Active Site J.Biol.Chem., 276, 2001
|
|
1PSD
| |
2HDH
| |
1YBA
| The active form of phosphoglycerate dehydrogenase | Descriptor: | 2-OXOGLUTARIC ACID, D-3-phosphoglycerate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | Authors: | Thompson, J.R, Banaszak, L.J. | Deposit date: | 2004-12-20 | Release date: | 2005-04-26 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.24 Å) | Cite: | Vmax Regulation through Domain and Subunit Changes. The Active Form of Phosphoglycerate Dehydrogenase Biochemistry, 44, 2005
|
|
1ALB
| |
2IFB
| |
1CBI
| APO-CELLULAR RETINOIC ACID BINDING PROTEIN I | Descriptor: | CELLULAR RETINOIC ACID BINDING PROTEIN I | Authors: | Thompson, J.R, Bratt, J.M, Banaszak, L.J. | Deposit date: | 1995-07-12 | Release date: | 1995-11-14 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet. J.Mol.Biol., 252, 1995
|
|
1F12
| L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH 3-HYDROXYBUTYRYL-COA | Descriptor: | 3-HYDROXYBUTANOYL-COENZYME A, L-3-HYDROXYACYL-COA DEHYDROGENASE | Authors: | Barycki, J.J, O'Brien, L.K, Strauss, A.W, Banaszak, L.J. | Deposit date: | 2000-05-18 | Release date: | 2000-09-27 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.4 Å) | Cite: | Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J.Biol.Chem., 275, 2000
|
|
1F14
| |
1F0Y
| L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH ACETOACETYL-COA AND NAD+ | Descriptor: | ACETOACETYL-COENZYME A, L-3-HYDROXYACYL-COA DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE | Authors: | Barycki, J.J, O'Brien, L.K, Strauss, A.W, Banaszak, L.J. | Deposit date: | 2000-05-17 | Release date: | 2000-09-01 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J.Biol.Chem., 275, 2000
|
|
1F17
| L-3-HYDROXYACYL-COA DEHYDROGENASE COMPLEXED WITH NADH | Descriptor: | 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, L-3-HYDROXYACYL-COA DEHYDROGENASE | Authors: | Barycki, J.J, O'Brien, L.K, Strauss, A.W, Banaszak, L.J. | Deposit date: | 2000-05-18 | Release date: | 2000-09-27 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase. J.Biol.Chem., 275, 2000
|
|
1IL0
| X-RAY CRYSTAL STRUCTURE OF THE E170Q MUTANT OF HUMAN L-3-HYDROXYACYL-COA DEHYDROGENASE | Descriptor: | 3-hydroxyacyl-CoA dehydrogenase, ACETOACETYL-COENZYME A, NICOTINAMIDE-ADENINE-DINUCLEOTIDE | Authors: | Barycki, J.J, O'Brien, L.K, Strauss, A.W, Banaszak, L.J. | Deposit date: | 2001-05-07 | Release date: | 2001-11-07 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. J.Biol.Chem., 276, 2001
|
|
2CMD
| |
1TIP
| THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE | Descriptor: | 6-O-phosphono-beta-D-fructofuranose, PHOSPHOENZYME INTERMEDIATE OF FRU-2,6-BISPHOSPHATASE | Authors: | Lee, Y.-H, Olson, T.W, Ogata, C.M, Levitt, D.G, Banaszak, L.J, Lange, A.J. | Deposit date: | 1997-05-28 | Release date: | 1998-01-28 | Last modified: | 2020-07-29 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Crystal structure of a trapped phosphoenzyme during a catalytic reaction. Nat.Struct.Biol., 4, 1997
|
|
2ANS
| |
1ADL
| ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH ARACHIDONIC ACID: X-RAY CRYSTALLOGRAPHIC AND TITRATION CALORIMETRY STUDIES | Descriptor: | ADIPOCYTE LIPID-BINDING PROTEIN, ARACHIDONIC ACID, PROPANOIC ACID | Authors: | Lalonde, J.M, Levenson, M, Roe, J.J, Bernlohr, D.A, Banaszak, L.J. | Deposit date: | 1994-03-25 | Release date: | 1994-12-20 | Last modified: | 2024-10-09 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Adipocyte lipid-binding protein complexed with arachidonic acid. Titration calorimetry and X-ray crystallographic studies. J.Biol.Chem., 269, 1994
|
|
1FBT
| THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE | Descriptor: | FRUCTOSE-2,6-BISPHOSPHATASE, PHOSPHATE ION | Authors: | Lee, Y.-H, Ogata, C, Pflugrath, J.W, Levitt, D.G, Sarma, R, Banaszak, L.J, Pilkis, S.J. | Deposit date: | 1996-03-08 | Release date: | 1997-07-23 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases. Biochemistry, 35, 1996
|
|
1HQS
| CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS | Descriptor: | CITRIC ACID, ISOCITRATE DEHYDROGENASE, R-1,2-PROPANEDIOL, ... | Authors: | Singh, S.K, Matsuno, K, LaPorte, D.C, Banaszak, L.J. | Deposit date: | 2000-12-19 | Release date: | 2001-07-25 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (1.55 Å) | Cite: | Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J.Biol.Chem., 276, 2001
|
|