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Structure of IDP90591

Crystal structure of tryptophanyl-tRNA synthetase from Yersinia pestis CO92

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CSGID target
IDP90591 
PDB Id
3N9I (NCBI MMDB) 
Authors
Nocek,B., Maltseva, N., Papazisi, L., Joachimiak, A. Anderson, W., CSGID,NIAID 
Responsible person
Boguslaw Nocek 
Responsible lab
Argonne National Laboratory 
Deposition Date
May 30, 2010 
Release Date
Jul 21, 2010 

Annotation

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Description
The crystal structure of ligand-free tryptophanyl-tRNA synthetase forms a dimer. It contain a conserved core domain that is involved in ATP binding (motif KMSKS, residue 207-211)and hydrolysis and combines with additional domains that determine the specificity of interactions with the tryptophan and tRNA.  
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
    GOL glycerol
    CA calcium ion

    Structure information

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    Unit cell parameters

    Space Group
    P 21 21 21  
    Unit Cell

    a=61.10Å, b=78.15Å, c=152.18Å
    α=90.00, β=90.00, γ=90.00  
    Solvent content
    47.57  
    Matthews coefficient
    2.35  

    Refinement

    Data for the highest resolution shell is in parentheses.
    Resolution range
    40.00-1.95Å (2.00-1.95Å)  
    Rall(%)
    16.9  
    Rwork(%)
    16.7 (22.2)  
    Rfree(%)
    20.6 (27.9)  
    Num. observed reflections
    53040 (3679)  
    Num. Rfree reflections
    2705 (192)  
    Completeness(%)
    98.7 (94.3)  

    Model parameters

    Num Atoms
    5684  
    Num Waters
    445  
    Num Hetatoms
    1  
    Model mean isotropic B factor (Å2)
    22.720  
    RMSD bond length (Å)
    0.016  
    RMSD bond angle
    1.420°  
    Filename uploaded
    90591-0528-10_refmac1-DEPOSIT.pdb (uploaded on May 30, 2010 8:20 PM)  
    Inserted
    May 30, 2010