6KJ9
| E. coli ATCase catalytic subunit mutant - G128/130A | Descriptor: | Aspartate carbamoyltransferase catalytic subunit | Authors: | Lei, Z, Zheng, J, Jia, Z.C. | Deposit date: | 2019-07-22 | Release date: | 2020-03-11 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development. Febs J., 287, 2020
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6KJB
| wild-type apo-form E. coli ATCase holoenzyme with an unusual open conformation of R167 | Descriptor: | Aspartate carbamoyltransferase catalytic subunit, Aspartate carbamoyltransferase regulatory chain, ZINC ION | Authors: | Wang, N, Lei, Z, Zheng, J, Jia, Z.C. | Deposit date: | 2019-07-22 | Release date: | 2020-06-03 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.06 Å) | Cite: | Conformational Plasticity of the Active Site Entrance inE. coliAspartate Transcarbamoylase and Its Implication in Feedback Regulation. Int J Mol Sci, 21, 2020
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6KJ8
| E. coli ATCase holoenzyme mutant - G166P (catalytic chain) | Descriptor: | Aspartate carbamoyltransferase catalytic subunit, Aspartate carbamoyltransferase regulatory chain, ZINC ION | Authors: | Lei, Z, Zheng, J, Jia, Z.C. | Deposit date: | 2019-07-22 | Release date: | 2020-03-11 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (3.011 Å) | Cite: | New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development. Febs J., 287, 2020
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3L04
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92P mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.5 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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3KZC
| Crystal structure of N-acetyl-L-ornithine transcarbamylase | Descriptor: | N-acetylornithine carbamoyltransferase, SULFATE ION | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. J.Biol.Chem., 280, 2005
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3KZM
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate | Descriptor: | GLYCEROL, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.95 Å) | Cite: | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64, 2006
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3KZO
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline | Descriptor: | GLYCEROL, N-ACETYL-L-NORVALINE, N-acetylornithine carbamoyltransferase, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64, 2006
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3KZK
| Crystal structure of acetylornithine transcarbamylase complexed with acetylcitrulline | Descriptor: | (S)-2-ACETAMIDO-5-UREIDOPENTANOIC ACID, N-acetylornithine carbamoyltransferase, SULFATE ION | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. J.Biol.Chem., 280, 2005
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3L06
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92V mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.81 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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3KZN
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with N-acetyl-L-ornirthine | Descriptor: | GLYCEROL, N-acetylornithine carbamoyltransferase, N~2~-ACETYL-L-ORNITHINE, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-08 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins, 64, 2006
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3L05
| Crystal structure of N-acetyl-L-ornithine transcarbamylase E92S mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline | Descriptor: | N-(3-CARBOXYPROPANOYL)-L-NORVALINE, N-acetylornithine carbamoyltransferase, PHOSPHORIC ACID MONO(FORMAMIDE)ESTER, ... | Authors: | Shi, D, Yu, X, Allewell, N.M, Tuchman, M. | Deposit date: | 2009-12-09 | Release date: | 2010-03-31 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Protein Sci., 16, 2007
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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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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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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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3LXM
| 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia pestis CO92 | Descriptor: | Aspartate carbamoyltransferase, TETRAETHYLENE GLYCOL | Authors: | Halavaty, A.S, Minasov, G, Dubrovska, I, Winsor, J, Shuvalova, L, Peterson, S, Anderson, W.F, Center for Structural Genomics of Infectious Diseases (CSGID) | Deposit date: | 2010-02-25 | Release date: | 2010-03-16 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | 2.00 Angstrom resolution crystal structure of a catalytic subunit of an aspartate carbamoyltransferase (pyrB) from Yersinia pestis CO92 To be Published
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3M4J
| Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-11 | Release date: | 2010-07-28 | Last modified: | 2023-11-22 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Reversible Post-Translational Carboxylation Modulates the Enzymatic Activity of N-Acetyl-l-ornithine Transcarbamylase. Biochemistry, 49, 2010
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1TUG
| Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP) | Descriptor: | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, CYTIDINE-5'-TRIPHOSPHATE, ... | Authors: | Stieglitz, K, Stec, B, Baker, D.P, Kantrowitz, E.R. | Deposit date: | 2004-06-24 | Release date: | 2004-07-20 | Last modified: | 2024-04-03 | Method: | X-RAY DIFFRACTION (2.1 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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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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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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3M4N
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302A mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-11 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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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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3M5D
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302R mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-12 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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3M5C
| Crystal structure of N-acetyl-L-ornithine transcarbamylase K302E mutant complexed with PALAO | Descriptor: | N-acetylornithine carbamoyltransferase, N~2~-acetyl-N~5~-(phosphonoacetyl)-L-ornithine, SULFATE ION | Authors: | Li, Y, Yu, X, Allewell, N.M, Tuchman, M, Shi, D. | Deposit date: | 2010-03-12 | Release date: | 2010-07-28 | Last modified: | 2023-09-06 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Reversible post-translational carboxylation modulates the enzymatic activity of N-acetyl-L-ornithine transcarbamylase. Biochemistry, 49, 2010
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