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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1FBP
| CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATASE COMPLEXED WITH FRUCTOSE 6-PHOSPHATE, AMP, AND MAGNESIUM | Descriptor: | 6-O-phosphono-beta-D-fructofuranose, ADENOSINE MONOPHOSPHATE, FRUCTOSE 1,6-BISPHOSPHATASE, ... | Authors: | Ke, H, Zhang, Y, Lipscomb, W.N. | Deposit date: | 1990-05-31 | Release date: | 1992-04-15 | Last modified: | 2020-07-29 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium. Proc.Natl.Acad.Sci.USA, 87, 1990
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2AIR
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1DCT
| DNA (CYTOSINE-5) METHYLASE FROM HAEIII COVALENTLY BOUND TO DNA | Descriptor: | CALCIUM ION, DNA (5'-D(*AP*CP*CP*AP*GP*CP*AP*GP*GP*(C49)P*CP*AP*CP*CP*AP*GP*TP*G)-3'), DNA (5'-D(*TP*CP*AP*CP*TP*GP*GP*TP*GP*GP*(C5M)P*CP*TP*GP*CP*TP*GP*G)-3'), ... | Authors: | Reinisch, K.M, Chen, L, Verdine, G.L, Lipscomb, W.N. | Deposit date: | 1995-05-17 | Release date: | 1995-09-15 | Last modified: | 2019-11-20 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing. Cell(Cambridge,Mass.), 82, 1995
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1FBC
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, FRUCTOSE 1,6-BISPHOSPHATASE, MAGNESIUM ION | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-14 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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1FBG
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-mannitol, FRUCTOSE 1,6-BISPHOSPHATASE, MANGANESE (II) ION | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-16 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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1FBF
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-mannitol, FRUCTOSE 1,6-BISPHOSPHATASE, MAGNESIUM ION | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-16 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.7 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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1FPB
| CRYSTAL STRUCTURE OF THE NEUTRAL FORM OF FRUCTOSE 1,6-BISPHOSPHATASE COMPLEXED WITH REGULATORY INHIBITOR FRUCTOSE 2,6-BISPHOSPHATE AT 2.6-ANGSTROMS RESOLUTION | Descriptor: | 2,6-di-O-phosphono-beta-D-fructofuranose, FRUCTOSE 1,6-BISPHOSPHATASE | Authors: | Liang, J.Y, Huang, S, Zhang, Y, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-02-03 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.6 Å) | Cite: | Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution. Proc.Natl.Acad.Sci.USA, 89, 1992
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1FBD
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, FRUCTOSE 1,6-BISPHOSPHATASE, MANGANESE (II) ION | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-16 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.9 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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1FBH
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 1,6-di-O-phosphono-alpha-D-fructofuranose, 1,6-di-O-phosphono-beta-D-fructofuranose, FRUCTOSE 1,6-BISPHOSPHATASE | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-16 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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1FBE
| CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE | Descriptor: | 2,5-anhydro-1,6-di-O-phosphono-D-glucitol, FRUCTOSE 1,6-BISPHOSPHATASE, ZINC ION | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Ke, H, Lipscomb, W.N. | Deposit date: | 1992-10-16 | Release date: | 1993-10-31 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (3 Å) | Cite: | Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase. Biochemistry, 32, 1993
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2AT2
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2CHT
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2CHS
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1FTA
| FRUCTOSE-1,6-BISPHOSPHATASE(D-FRUCTOSE-1,6-BISPHOSPHATE, 1-PHOSPHOHYDROLASE) (E.C.3.1.3.11) COMPLEXED WITH THE ALLOSTERIC INHIBITOR AMP | Descriptor: | ADENOSINE MONOPHOSPHATE, FRUCTOSE-1,6-BISPHOSPHATASE | Authors: | Zhang, Y, Liang, J.-Y, Huang, S, Lipscomb, W.N. | Deposit date: | 1993-09-27 | Release date: | 1995-11-14 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure. J.Biol.Chem., 269, 1994
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