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Structure of IDP91191

Crystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, ATP-bound

Edit deposit information
CSGID target
IDP91191 
PDB Id
3R78 (NCBI MMDB
Authors
P.J.Stogios,K.Tan,E.Evdokimova,E.Egorova,R.Di Leo,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid),Ontario Centre For Structural Proteomics (Ocsp) 
Responsible person
Peter Stogios 
Responsible lab
University of Calgary 
Deposition Date
Mar 22, 2011 
Release Date
Apr 13, 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 ATP-bound structure of APH(3')-Ia, an enzyme that acts on kanamycin and other aminoglycosides.  
Functional assignment
kinase 

Ligands

Ligand code Name Ligand type
CL CHLORIDE ION crystallization
CA crystallization
NA Sodium ion crystallization
ATP adenosine-5'-triphosphate biological
ACT acetate crystallization
MSE modified residue
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
C 2 2 21  
Unit Cell

a=85.36Å, b=152.47Å, c=165.57Å
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
43.67-2.40Å (2.49-2.40Å)  
Rall(%)
19.5 
Rwork(%)
19.3 (29.2) 
Rfree(%)
24.7 (33.7) 
Num. observed reflections
77956 (6615) 
Num. Rfree reflections
3281 (271) 
Completeness(%)
91.6 (81.0) 

Model parameters

Num Atoms
6296  
Num Waters
188  
Num Hetatoms
507  
Model mean isotropic B factor
60.230Å2  
RMSD bond length
0.009Å  
RMSD bond angle
1.222°  
RMSD dihedral angle
15.767°
 
Filename uploaded
3R78.pdb (uploaded on Apr 14, 2011 9:04 AM)  
Inserted
Apr 14, 2011