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Structure of IDP01801

Crystal Structure of Glutaredoxin 1 from Francisella tularensis Complexed with Cacodylate

Edit deposit information
CSGID target
IDP01801 
PDB Id
3MSZ (NCBI MMDB
Authors
N.Maltseva,Y.Kim,K.Kwon,W.F.Anderson,A.Joachimiak 
Responsible person
Natalia Maltseva 
Responsible lab
Argonne National Laboratory 
Deposition Date
Apr 29, 2010 
Release Date
May 19, 2010 

Annotation

Description
Glutaredoxins, also known as thioltransferases (disulphide reductases), are small proteins with function of an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Similar to thioredoxin, glutaredoxin contains disulphide bond in the active center. It exists in either a reduced or an oxidized form and in the present structure two cysteine residues are in alternative conformation with one of them forming an intramolecular disulphide bond. This structure contains a cacodylate molecule. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
GTT glutathione biological
CAC cacodylate ion
GOL
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 32 2 1  
Unit Cell

a=49.14Å, b=49.14Å, c=140.20Å
α=90.00, β=90.00, γ=120.00 
Solvent content
47.4  
Matthews coefficient
2.34  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
40.72-2.05Å (2.26-2.05Å)  
Rall(%)
17.5 
Rwork(%)
17.3 (19.1) 
Rfree(%)
22.3 (27.5) 
Num. observed reflections
13487 (3111) 
Num. Rfree reflections
655 (149) 
Completeness(%)
99.5 (99.0) 

Model parameters

Num Atoms
1553  
Num Waters
86  
Num Hetatoms
51  
Model mean isotropic B factor
34.130Å2  
RMSD bond length
0.013Å  
RMSD bond angle
1.329°  
RMSD dihedral angle
18.298°
 
Filename uploaded
dep.pdb (uploaded on Apr 30, 2010 12:32 PM)  
Inserted
Apr 30, 2010