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Structure of IDP90832

Thioredoxin-disulfide reductase from Campylobacter jejuni.

Edit deposit information
CSGID target
IDP90832 
PDB Id
3R9U (NCBI MMDB
Authors
J.Osipiuk,M.Zhou,K.Kwon,K.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Mar 25, 2011 
Release Date
Apr 06, 2011 

Annotation

Description
Thioredoxin-disulfide reductases (TrxR) catalyze the reduction of thioredoxin (Trx) using NADPH as a reducing agent. These 3 components comprise 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. There are numerous systems with thiol-dependent redox mechanisms, which are related to important pathological states and human diseases. Thioredoxin reductase is upregulated in several types of cancer, including malignant mesothelioma, thus it is a good target for anti-tumor therapy. 
Functional assignment
Reductase 

Ligands

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

Structure information

Unit cell parameters

Space Group
C 2 2 2  
Unit Cell

a=154.01Å, b=163.57Å, c=66.88Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
38.50-2.36Å (2.42-2.36Å)  
Rall(%)
19.6 
Rwork(%)
19.3 (26.8) 
Rfree(%)
24.7 (29.0) 
Num. observed reflections
35055 (2482) 
Num. Rfree reflections
1752 (138) 
Completeness(%)
99.3 (95.9) 

Model parameters

Num Atoms
4932  
Num Waters
84  
Num Hetatoms
0  
Model mean isotropic B factor
51.790Å2  
RMSD bond length
0.019Å  
RMSD bond angle
1.806°  
Filename uploaded
idp90823.pdb (uploaded on Mar 25, 2011 8:01 PM)  
Inserted
Mar 25, 2011