Brand  (β version)

PDB ID: 1RAA

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Ligands
Code Name Style Show Link
CTP Cytidine-5'-triphosphate PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
Code Name Emphasize
Modification
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Structure summary

Code : 1RAA   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : CRYSTAL STRUCTURE OF CTP-LIGATED T STATE ASPARTATE TRANSCARBAMOYLASE AT 2.5 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ATCASE MUTANTS AND THE MECHANISM OF NEGATIVE COOPERATIVITY
Release Data : 1994-01-31
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
1 Escherichia coli  (taxid:83333)
strain: K12
gene: pyrB, b4245, JW4204
mol_id organism_scientific
2 Escherichia coli  (taxid:83333)
strain: K12
gene: pyrI, b4244, JW4203
Authors : Kosman, R.P., Gouaux, J.E., Lipscomb, W.N.
Keywords : TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.5 Å )
Citation :

Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity.

Kosman, R.P.,Gouaux, J.E.,Lipscomb, W.N.
(1993)  Proteins  15 : 147 - 176

PubMed: 8441751
DOI: 10.1002/prot.340150206

Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase: Crystal Structures of the Unligated and ATP-and Ctp-Complexed Enzymes at 2.6 Angstroms Resolution

Stevens, R.C.,Gouaux, J.E.,Lipscomb, W.N.
(1990)  Biochemistry  29 : 7691

Structural Asymmetry in the Ctp-Liganded Form of Aspartate Carbamoyltransferase from Escherichia Coli

Kim, K.H.,Pan, Z.,Honzatko, R.B.  et al.
(1987)  J.Mol.Biol.  196 : 853

Location of Amino Acid Alterations in Mutants of Aspartate Transcarbamoylase: Structural Aspects of Interallelic Complementation

Schachman, H.K.,Pauza, C.D.,Navre, M.  et al.
(1984)  Proc.Natl.Acad.Sci.USA  81 : 115

Nucleotide Sequence of the Structural Gene (Pyrb) that Encodes the Catalytic Polypeptide of Aspartate Transcarbamoylase of Escherichia Coli

Hoover, T.A.,Roof, W.D.,Foltermann, K.F.  et al.
(1983)  Proc.Natl.Acad.Sci.USA  80 : 2462

Amino Acid Sequence of the Catalytic Subunit of Aspartate Transcarbamoylase from Escherichia Coli

Konigsberg, W.H.,Henderson, L.
(1983)  Proc.Natl.Acad.Sci.USA  80 : 2467

Reaction

Chain : A, C
UniProt : P0A786 (PYRB_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L- aspartate + phosphate 2.1.3.2 HAMAP- Rule:MF_00001, PubMed:13319326
-
Chain : B, D
UniProt : P0A7F3 (PYRI_ECOLI)
Reaction : -