Home    Target List    Selection    Community Requests    Clones    Screenings    XML files    Diffraction Images    Progress    Homolog Search    Clustering    Statistics    News    Help    Log In
To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP02821

Crystal Structure of ATP-dependent Clp Protease Subunit P from Francisella tularensis

(tree view)
Edit deposit information
CSGID target
IDP02821 
PDB Id
3P2L (NCBI MMDB) 
Authors
Y.Kim,M.Zhou,M.Gu,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Oct 02, 2010 
Release Date
Oct 20, 2010 

Annotation

Edit this annotation | Download molsoft presentation
Description
The Clp protease is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin. It exists as a heterodimer of ATP-binding regulatory A and catalytic P subunits, both of which are required for effective levels of protease activity in the presence of ATP. The Clp protease subunit P from Francisella tularensis assembled to two stacked heptameric rings that enclose a large chamber containing the protease active site including catalytic triad, Ser, His, and Glu/Asp. The N-terminal region, whose sequence is well conserved, is known to form a flexible loop protruding from the apical surface and associate with ATPase ClpA and ClpX, however, is disordered in the structure.  
Functional assignment
 
Slides:
  • Asymmetric unit
  • Biological unit
  • B-factors distribution
  • B-factors distribution on the surface
  • Homolog superposition
    • Presentation Controlls:
    rotate
    with the [Left]-mouse
    drag
    with the [Middle]-mouse (or with [Ctrl]-key pressed)
    zoom
    with the [Left]-mouse in the left zone of the window: zoom-up, unzoom-down
    clipping
    with the [Left]-mouse in the right zone of the window

    Presentation Options:
    background color:
    black, white
    ribbon style:
    normal, smooth
    ribbon color:
    secondary structure, N to C, molecule

    Ligands

    Ligand code Name Ligand type
    PO4 phosphate ion biological
    GOL glycerol crystallization
    PEG di(hydroxyethyl)ether crystallization
    EDO 1,2-ethanediol crystallization
    MG magnesium ion crystallization
    MSE selenomethionine modified residue

    Structure information

    View structure information | Edit structure information (upload a PDB file)

    Unit cell parameters

    Space Group
    P 21 21 2  
    Unit Cell

    a=120.52Å, b=128.82Å, c=98.03Å
    α=90.00, β=90.00, γ=90.00  
    Solvent content
    48.35  
    Matthews coefficient
    2.38  

    Refinement

    Data for the highest resolution shell is in parentheses.
    Resolution range
    40.45-2.30Å (2.38-2.30Å)  
    Rall(%)
    18.8  
    Rwork(%)
    18.6 (23.2)  
    Rfree(%)
    22.6 (30.1)  
    Num. observed reflections
    71785 (6500)  
    Num. Rfree reflections
    3625 (322)  
    Completeness(%)
    99.2 (96.0)  

    Model parameters

    Num Atoms
    10049  
    Num Waters
    349  
    Num Hetatoms
    698  
    Model mean isotropic B factor (Å2)
    60.140  
    RMSD bond length (Å)
    0.011  
    RMSD bond angle
    1.294°  
    RMSD dihedral angle
    17.09°
     
    Filename uploaded
    dep.pdb (uploaded on Oct 05, 2010 7:49 AM)  
    Inserted
    Oct 05, 2010