Structure of IDP91187

Crystal structure of aminoglycoside phosphotransferase APH(2")-Ib/APH(2'')-IIa, apo form

Edit deposit information
CSGID target
IDP91187 
PDB Id
3UZR (NCBI MMDB
Authors
P.J.Stogios,G.Minasov,A.U.Singer,K.Tan,B.Nocek,E.Evdokimova,E.Egorova,R.Di Leo,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Peter Stogios 
Responsible lab
University of Calgary 
Deposition Date
Dec 07, 2011 
Release Date
Dec 21, 2011 

Annotation

Description
Aminoglycoside phosphotransferase (APH) enzymes act in a substrate- and position-specific manner and confer resistance to the activity of various aminoglycoside antibiotics. APH enzymes show a eukaryotic protein kinase-like fold with an insertion that takes part in substrate recognition. This is the apo structure of APH(2'')-Ib, an enzyme that acts on gentamicin, kanamycin, neomycin and other aminoglycosides. 
Functional assignment
kinase 

Ligands

Ligand code Name Ligand type
EDO crystallization
MG MAGNESIUM ION crystallization
MSE modified residue
PEG crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 2 21 21  
Unit Cell

a=60.72Å, b=62.22Å, c=89.73Å
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
19.93-1.95Å (2.00-1.95Å)  
Rall(%)
19.6 
Rwork(%)
19.4 (28.1) 
Rfree(%)
24.5 (32.2) 
Num. observed reflections
23269 (1268) 
Num. Rfree reflections
1186 (60) 
Completeness(%)
91.6 (70.1) 

Model parameters

Num Atoms
2509  
Num Waters
261  
Num Hetatoms
360  
Model mean isotropic B factor
29.450Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.251°  
Filename uploaded
3UZR.pdb (uploaded on Feb 14, 2012 8:55 AM)  
Inserted
Mar 23, 2011