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Structure of IDP01750

Crystal Structure of the C194A mutant of 7-cyano-7-deazaguanine reductase, QueF from Vibrio cholerae complexed with preQ1

Edit deposit information
CSGID target
IDP01750 
PDB Id
3RZP (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
May 12, 2011 
Release Date
Jun 29, 2011 

Annotation

Description
This enzyme 7-cyano-7-deazaguanine reductase or QueF from Vibrio cholerae, is responsible for the complete reduction of a nitrile (CºN) bond to a primary amine (H2C–NH2). The QueF protein is homologous to the GTP cyclohydrolases I consisting of multiple tunneling-fold (T-fold). The protein containing a point mutation of Cys-194 (catalytic residue) to Ala-194 was crystallized and soaked with the product molecule preQ1. The 2.0 A dimeric structure revealed the bound preQ1 in the active site patch. 
Functional assignment
reductase 

Ligands

Ligand code Name Ligand type
PRF 7-deaza-7-aminomethyl-guanine biological
MSE SELENOMETHIONINE modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 1  
Unit Cell

a=71.32Å, b=71.19Å, c=71.46Å
α=110.43, β=119.22, γ=99.33 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
35.02-2.00Å (2.03-2.00Å)  
Rall(%)
17.4 
Rwork(%)
17.1 (27.3) 
Rfree(%)
22.1 (34.0) 
Num. observed reflections
71353 (2590) 
Num. Rfree reflections
3617 (150) 
Completeness(%)
95.7 (91.0) 

Model parameters

Num Atoms
8438  
Num Waters
470  
Num Hetatoms
534  
Model mean isotropic B factor
43.130Å2  
RMSD bond length
0.007Å  
RMSD bond angle
1.217°  
RMSD dihedral angle
15.726°
 
Filename uploaded
dep.pdb (uploaded on May 12, 2011 9:30 AM)  
Inserted
May 12, 2011