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Ligands
Code Name Style Show Link
AL0 3-[hydroxy(nitroso)amino]-L-alanine
CP Phosphoric acid mono(formamide)ester
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 2AIR   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme
Release Data : 2006-01-24
Compound :
mol_id molecule chains synonym
1 Aspartate carbamoyltransferase catalytic chain A,G Aspartate transcarbamylase, ATCase
ec: 2.1.3.2
mol_id molecule chains
2 Aspartate carbamoyltransferase regulatory chain B,H
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 : Huang, J., Lipscomb, W.N.
Keywords : Aspartate Transcarbamylase, Alanosine, Carbamyl Phosphate, T-state, Transferase
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

T-State Active Site of Aspartate Transcarbamylase: Crystal Structure of the Carbamyl Phosphate and l-Alanosine Ligated Enzyme

Huang, J.,Lipscomb, W.N.
(2006)  Biochemistry  45 : 346 - 352

PubMed: 16401065
DOI: 10.1021/bi051543u

Chain : A, G
UniProt : P0A786 (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, H
UniProt : P0A7F3 (PYRI_ECOLI)
Reaction : -
Cofactor: Evidence: Note:
Zn(2+) - Binds 1 zinc ion per subunit.