4CSM
| YEAST CHORISMATE MUTASE + TYR + ENDOOXABICYCLIC INHIBITOR | Descriptor: | 8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID, CHORISMATE MUTASE, TYROSINE | Authors: | Straeter, N, Schnappauf, G, Braus, G, Lipscomb, W.N. | Deposit date: | 1997-07-14 | Release date: | 1998-01-14 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Structure, 5, 1997
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2FBP
| STRUCTURE REFINEMENT OF FRUCTOSE-1,6-BISPHOSPHATASE AND ITS FRUCTOSE 2,6-BISPHOSPHATE COMPLEX AT 2.8 ANGSTROMS RESOLUTION | Descriptor: | FRUCTOSE 1,6-BISPHOSPHATASE | Authors: | Ke, H, Thorpe, C.M, Seaton, B.A, Marcus, F, Lipscomb, W.N. | Deposit date: | 1990-06-07 | Release date: | 1992-04-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution. J.Mol.Biol., 212, 1990
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1SPI
| CRYSTAL STRUCTURE OF SPINACH CHLOROPLAST FRUCTOSE-1,6-BISPHOSPHATASE AT 2.8 ANGSTROMS RESOLUTION | Descriptor: | FRUCTOSE 1,6-BISPHOSPHATASE | Authors: | Villeret, V, Huang, S, Zhang, Y, Xue, Y, Lipscomb, W.N. | Deposit date: | 1994-12-14 | Release date: | 1995-02-27 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 A resolution. Biochemistry, 34, 1995
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1BLL
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2CSM
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1R0C
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1BPM
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1BPN
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1RAE
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAF
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAH
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAC
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAG
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAD
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAB
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAI
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1RAA
| CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Kosman, R.P, Gouaux, J.E, Lipscomb, W.N. | Deposit date: | 1992-08-14 | Release date: | 1994-01-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins, 15, 1993
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1Q95
| Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... | Authors: | Huang, J, Lipscomb, W.N. | Deposit date: | 2003-08-22 | Release date: | 2004-06-08 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2.46 Å) | Cite: | Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate Biochemistry, 43, 2004
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1R0B
| Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CITRATE ANION, ... | Authors: | Huang, J, Lipscomb, W.N. | Deposit date: | 2003-09-19 | Release date: | 2004-06-08 | Last modified: | 2023-08-23 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate Biochemistry, 43, 2004
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4FBP
| CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM) | Descriptor: | ADENOSINE MONOPHOSPHATE, FRUCTOSE 1,6-BISPHOSPHATASE | Authors: | Ke, H, Zhang, Y, Liang, J.-Y, Lipscomb, W.N. | Deposit date: | 1991-02-11 | Release date: | 1992-07-15 | Last modified: | 2024-02-28 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry, 30, 1991
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1FPG
| STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, ADENOSINE MONOPHOSPHATE, FRUCTOSE 1,6-BISPHOSPHATASE, ... | Authors: | Villeret, V, Huang, S, Zhang, Y, Lipscomb, W.N. | Deposit date: | 1994-12-15 | Release date: | 1995-02-27 | Last modified: | 2020-07-29 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Biochemistry, 34, 1995
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1FPI
| FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND POTASSIUM IONS (100 MM) | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, ADENOSINE MONOPHOSPHATE, FRUCTOSE-1,6-BISPHOSPHATASE, ... | Authors: | Villeret, V, Lipscomb, W.N. | Deposit date: | 1995-06-02 | Release date: | 1996-06-20 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Proc.Natl.Acad.Sci.USA, 92, 1995
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1FPJ
| FRUCTOSE-1,6-BISPHOSPHATASE (D-FRUCTOSE-1,6-BISPHOSPHATE 1-PHOSPHOHYDROLASE) COMPLEXED WITH AMP, 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE, THALLIUM (10 MM) AND LITHIUM IONS (10 MM) | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, ADENOSINE MONOPHOSPHATE, FRUCTOSE-1,6-BISPHOSPHATASE, ... | Authors: | Villeret, V, Lipscomb, W.N. | Deposit date: | 1995-06-02 | Release date: | 1996-06-20 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Proc.Natl.Acad.Sci.USA, 92, 1995
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1FPE
| STRUCTURAL ASPECTS OF THE ALLOSTERIC INHIBITION OF FRUCTOSE-1,6-BISPHOSPHATASE BY AMP: THE BINDING OF BOTH THE SUBSTRATE ANALOGUE 2,5-ANHYDRO-D-GLUCITOL-1,6-BISPHOSPHATE AND CATALYTIC METAL IONS MONITORED BY X-RAY CRYSTALLOGRAPHY | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, ADENOSINE MONOPHOSPHATE, FRUCTOSE 1,6-BISPHOSPHATASE, ... | Authors: | Villeret, V, Huang, S, Zhang, Y, Lipscomb, W.N. | Deposit date: | 1994-12-15 | Release date: | 1995-02-27 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography. Biochemistry, 34, 1995
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1FRP
| CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE-2,6-BISPHOSPHATE, AMP AND ZN2+ AT 2.0 ANGSTROMS RESOLUTION. ASPECTS OF SYNERGISM BETWEEN INHIBITORS | Descriptor: | 2,6-di-O-phosphono-beta-D-fructofuranose, ADENOSINE MONOPHOSPHATE, FRUCTOSE 1,6-BISPHOSPHATASE, ... | Authors: | Xue, Y, Huang, S, Liang, J.-Y, Zhang, Y, Lipscomb, W.N. | Deposit date: | 1994-08-26 | Release date: | 1994-11-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors. Proc.Natl.Acad.Sci.USA, 91, 1994
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