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Ligands
Code Name Style Show Link
CP Phosphoric acid mono(formamide)ester
CTP Cytidine-5'-triphosphate
NA Sodium ion
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 1ZA2   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution
Release Data : 2005-06-07
Compound :
mol_id molecule chains synonym
1 Aspartate carbamoyltransferase catalytic chain A,C Aspartate transcarbamylase, ATCase
ec: 2.1.3.2
mol_id molecule chains
2 Aspartate carbamoyltransferase regulatory chain B,D
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
gene: PYRB
expression_system_strain: EK1104
expression_system_vector_type: plasmid
expression_system_plasmid: pEK54
mol_id organism_scientific expression_system
2 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
gene: PYRI
expression_system_strain: EK1104
expression_system_vector_type: plasmid
expression_system_plasmid: pEK54
Authors : Wang, J., Stieglitz, K.A., Cardia, J.P., Kantrowitz, E.R.
Keywords : ordered substrate binding, cooperativity, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase

Wang, J.,Stieglitz, K.A.,Cardia, J.P.  et al.
(2005)  Proc.Natl.Acad.Sci.Usa  102 : 8881 - 8886

PubMed: 15951418
DOI: 10.1073/pnas.0503742102

Chain : A, C
UniProt : P00479 (PYRB_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+) 2.1.3.2 HAMAP-Rule:MF_00001, PubMed:13319326
-
Chain : B, D
UniProt : P00478 (PYRI_ECOLI)
Reaction : -
Cofactor: Evidence: Note:
Zn(2+) - Binds 1 zinc ion per subunit.