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PDBe Entry: 1d09 
ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 2.1 Å, R-factor: 20.3%, Free R-factor: 23.4%, Spacegroup: P 3 2 1
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28/01/2000, deposition: 09/09/1999, last revision: 24/02/2009
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Jin, L.; Stec, B.; Lipscomb, W.N.; Kantrowitz, E.R.
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Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.
PROTEINS vol:37, pag:729-742 (1999) [PubMed ID 10651286 ]
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PROTEIN-INHIBITOR COMPLEX ASPARTATE TRANSCARBAMOYLASE ASPARTATE TRANSCARBAMYLASE, TRANSFERASE
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2.1.3.2 ExPASy BRENDA (A C)
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Escherichia coli 562(A C B D)
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Aspartate carbamoyltransferase catalytic chain (EC 2.1.3.2) (Aspartate transcarbamylase) (ATCase) P0A786 (A C)
Aspartate carbamoyltransferase regulatory chain P0A7F3 (B D)
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A, B, C, D
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8atc
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| A, C |
ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN |
Protein |
P0A786 (PYRB_ECOLI)
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310 |
100% |
| B, D |
ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN |
Protein |
P0A7F3 (PYRI_ECOLI)
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153 |
100% |
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| B, D |
ZINC ION |
ZN
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| A, C |
N-(PHOSPHONACETYL)-L-ASPARTIC ACID |
PAL
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