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Structure of IDP02453

Crystal Structure of Maltose O-Acetyl transferase Complexed with Acetyl Coenzyme A from Bacillus anthracis

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CSGID target
IDP02453 
PDB Id
3IGJ (NCBI MMDB) 
Authors
Maltseva, N., Kim, Y., Papazisi, L., Anderson, W., Joachimiak, A., CSGID 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jul 27, 2009 
Release Date
Aug 04, 2009 

Annotation

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Description
This maltose O-acetyltransferase, a member of the hexapeptide-repeat family with a trimeric left-handed parallel beta-helix, transfers an acetyl group from acetyl-CoA to a sugar moiety. In the structure, CoA molecules are located between the two beta-helical chains. 
Functional assignment
 
Slides:
  • Asymmetric unit
  • Biological unit
  • B-factors distribution
  • B-factors distribution on the surface
  • Homolog superposition
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    secondary structure, N to C, molecule

    Ligands

    Ligand code Name Ligand type
    SO4 sulfate ion
    GOL glycerol
    FMT formic acid
    ACX alpha-cyclodextrin (cyclohexa-amylose)
    MSE selenomethionine modified residue

    Structure information

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    Unit cell parameters

    Space Group
    P 41 21 2  
    Unit Cell

    a=121.97Å, b=121.97Å, c=142.44Å
    α=90.00, β=90.00, γ=90.00  
    Solvent content
    71  
    Matthews coefficient
    4.24  

    Refinement

    Data for the highest resolution shell is in parentheses.
    Resolution range
    41.59-2.60Å (2.68-2.60Å)  
    Rall(%)
    17.5  
    Rwork(%)
    17.3 (23.1)  
    Rfree(%)
    21.3 (32.7)  
    Num. observed reflections
    34815 (2618)  
    Num. Rfree reflections
    1765 (133)  
    Completeness(%)
    98.3 (96.0)  

    Model parameters

    Num Atoms
    4731  
    Num Waters
    176  
    Num Hetatoms
    0  
    Model mean isotropic B factor (Å2)
    52.620  
    RMSD bond length (Å)
    0.011  
    RMSD bond angle
    1.437°  
    RMSD dihedral angle
    20.667°
     
    Filename uploaded
    dep1w.pdb (uploaded on Jul 31, 2009 8:36 AM)  
    Inserted
    Jul 31, 2009