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Structure of IDP01793

Putative thioredoxin protein from Salmonella typhimurium.

Edit deposit information
CSGID target
IDP01793 
PDB Id
3QDN (NCBI MMDB
Authors
J.Osipiuk,M.Zhou,K.Kwon,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jan 18, 2011 
Release Date
Feb 09, 2011 

Annotation

Description
Thioredoxins (Trx) are proteins that act as antioxidants catalyzing the reduction of other proteins. Thioredoxin, together with thioredoxin reductase (TrxR) and NADPH, comprises the thioredoxin system. The system is ubiquitous from Archea to man and supports several processes crucial for cell function, cell proliferation, antioxidant defense and redox-regulated signaling cascades. Multiple in vitro substrates for thioredoxin have been identified, including ribonuclease, choriogonadotropins, coagulation factors, glucocorticoid receptor, and insulin. Amino-acid sequence analysis suggests that the presented protein contains a redox-inactive Trx-like domain. 
Functional assignment
Oxidoreductase 

Ligands

Ligand code Name Ligand type
MSE selenomethionine modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=58.23Å, b=62.55Å, c=79.52Å
α=90.00, β=98.66, γ=90.00 
Solvent content
44.42  
Matthews coefficient
2.21  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
35.80-2.09Å (2.15-2.09Å)  
Rall(%)
24.5 
Rwork(%)
24.2 (33.4) 
Rfree(%)
30.2 (38.3) 
Num. observed reflections
32236 (1430) 
Num. Rfree reflections
1611 (73) 
Completeness(%)
96.3 (57.9) 

Model parameters

Num Atoms
4710  
Num Waters
94  
Num Hetatoms
0  
Model mean isotropic B factor
30.630Å2  
RMSD bond length
0.016Å  
RMSD bond angle
1.578°  
Filename uploaded
idp01793.pdb (uploaded on Jan 18, 2011 7:17 PM)  
Inserted
Jan 18, 2011