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Structure of IDP02821

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

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

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
 

Ligands

Ligand code Name Ligand type
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on biological
GOL glycerol crystallization
PEG crystallization
EDO ethylene diol crystallization
MG magnesium crystallization
MSE modified residue

Structure information

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
60.140Å2  
RMSD bond length
0.011Å  
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