Brand  (β version)

PDB ID: 3KZO

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
AN0 N-acetyl-L-norvaline PoSSuM
CP Phosphoric acid mono(formamide)ester PoSSuM
GOL Glycerol PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
KCX Lysine nz-carboxylic acid
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3KZO   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline
Release Data : 2010-03-31
Compound :
mol_id molecule chains synonym
1 N-acetylornithine carbamoyltransferase A AOTCase
ec: 2.1.3.9
Source :
mol_id organism_scientific expression_system
1 Xanthomonas campestris pv. campestris  (taxid:190485) Escherichia coli  (taxid:469008)
strain: ATCC 33913
gene: argF, argF', XCC2249
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET28a
Authors : Shi, D., Yu, X., Allewell, N.M., Tuchman, M.
Keywords : Transcarbamylase, Amino-acid biosynthesis, Arginine biosynthesis, Cytoplasm, Transferase
Exp. method : X-RAY DIFFRACTION ( 1.900 Å )
Citation :

Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.

Shi, D.,Yu, X.,Roth, L.  et al.
(2006)  Proteins  64 : 532 - 542

PubMed: 16741992
DOI: 10.1002/prot.21013

Reaction

Chain : A
UniProt : Q8P8J2 (AOTC_XANCP)
Reaction: EC: Evidence:
Physiological Direction:
N(2)-acetyl-L-ornithine + carbamoyl phosphate = N(2)-acetyl-L- citrulline + phosphate + H(+) 2.1.3.9 PubMed:16585758
left-to-right