Structure of IDP91802

Crystal structure of Disulfide Bond Oxidoreductase DsbA1 from Legionella pneumophila

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CSGID target
IDP91802 
PDB Id
4JRR (NCBI MMDB
Authors
I.A.Shumilin,M.Jameson-Lee,M.Cymborowski,M.J.Domagalski,O.Chertihin,Z.Z.Kpadeh,A.J.Yeh,P.S.Hoffman,W.F.Anderson,W.Minor,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Igor Shumilin 
Responsible lab
University of Virginia 
Deposition Date
Mar 21, 2013 
Release Date
Apr 24, 2013 

Annotation

Description
The DSB oxidoreductase family is part of the thioredoxin (TRX) super family of proteins, which are defined by the presence of one or more thioredoxin folds. These enzymes participate in disulfide bond formation through a conserved Cys-X-X-Cys (CXXC) active site motif, and can either reduce or oxidize target substrates. DsbA catalyzes the formation of consecutive disulfide bonds in nascent polypeptides entering the periplasm. 
Functional assignment
Disulfide Bond Oxidoreductase 

Ligands

Ligand code Name Ligand type
GOL crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=55.88Å, b=80.14Å, c=66.26Å
α=90.00, β=92.86, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
36.98-1.88Å (1.93-1.88Å)  
Rall(%)
16.4 
Rwork(%)
16.2 (24.1) 
Rfree(%)
20.5 (30.7) 
Num. observed reflections
47488 (3486) 
Num. Rfree reflections
2421 (154) 
Completeness(%)
99.9 (98.8) 

Model parameters

Num Atoms
4544  
Num Waters
376  
Num Hetatoms
414  
Model mean isotropic B factor
32.920Å2  
RMSD bond length
0.019Å  
RMSD bond angle
1.808°  
Filename uploaded
hkl_refine_53.pdb (uploaded on Mar 21, 2013 7:42 PM)  
Inserted
Mar 21, 2013