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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1SKU
 | | E. coli Aspartate Transcarbamylase 240's Loop Mutant (K244N) | | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, MALONATE ION, ... | | Authors: | Alam, N, Stieglitz, K.A, Caban, M.D, Gourinath, S, Tsuruta, H, Kantrowitz, E.R. | | Deposit date: | 2004-03-05 | | Release date: | 2004-03-30 | | Last modified: | 2023-08-23 | | Method: | X-RAY DIFFRACTION (2.6 Å) | | Cite: | 240s Loop Interactions Stabilize the T State of Escherichia coli Aspartate Transcarbamoylase.
J.Biol.Chem., 279, 2004
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1TU0
 | | Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide | | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, PHOSPHONOACETAMIDE, ... | | Authors: | Stieglitz, K, Stec, B, Baker, D.P, Kantrowitz, E.R. | | Deposit date: | 2004-06-23 | | Release date: | 2004-07-20 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (2.55 Å) | | Cite: | Monitoring the Transition from the T to the R State in E.coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States.
J.Mol.Biol., 341, 2004
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1TTH
 | | Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA) | | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... | | Authors: | Stieglitz, K, Stec, B, Baker, D.P, Kantrowitz, E.R. | | Deposit date: | 2004-06-22 | | Release date: | 2004-07-20 | | Last modified: | 2023-08-23 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | Monitoring the Transition from the T to the R State in E.coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States.
J.Mol.Biol., 341, 2004
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