Brand  (β version)

  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
03S Methanesulfonic acid
NA Sodium ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 5UG1   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Structure of Streptococcus pneumoniae peptidoglycan O-acetyltransferase A (OatA) C-terminal catalytic domain with methylsulfonyl adduct
Release Data : 2017-10-25
Compound :
mol_id molecule chains
1 Acyltransferase A
ec: 2.3.1.-
mutation: UNP residues 427-605
Source :
mol_id organism_scientific expression_system
1 Streptococcus pneumoniae  (taxid:1313) Escherichia coli  (taxid:469008)
gene: oatA_2, oatA, ERS020148_01611, ERS021300_00524, ERS022045_04974
expression_system_strain: BL21(DE3)
Authors : Sychantha, D., Jones, C., Little, D.J., Moynihan, P.J., Robinson, H., Galley, N.F., Roper, D.I., Dowson, C.G., Howell, P.L., Clarke, A.J.
Keywords : Transferase, atypical alpha/beta hydrolase fold, catalytic triad, covalent complex
Exp. method : X-RAY DIFFRACTION ( 2.100 Å )
Citation :

In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA).

Sychantha, D.,Jones, C.S.,Little, D.J.  et al.
(2017)  PLoS Pathog.  13 : e1006667 - e1006667

PubMed: 29077761
DOI: 10.1371/journal.ppat.1006667

Chain : A
UniProt : A0A0T8LL95
Reaction : -