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Structure of IDP01350

Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor

Edit deposit information
CSGID target
IDP01350 
PDB Id
3EEV (NCBI MMDB
Authors
Y.Kim,N.Maltseva,K.Kwon,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Youngchang Kim 
Responsible lab
Argonne National Laboratory 
Deposition Date
Sep 05, 2008 
Release Date
Sep 16, 2008 

Annotation

Description
This enzyme, responsible for chloramphenicol resistance in bacteria by detoxifying the antibiotics chloramphenicol, transfers an acetyl group from acetyl-CoA to chloramphenicol, which prevents chloramphenicol from binding to ribosomes. The enzyme is a trimer of protein chains comprising of a left-handed β-helical domain and α small three a-helix domain. The binding sites for CoA and chloramphenicol are located in between the two protein chains. This structure does not contain ligands.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
MPD

Structure information

Unit cell parameters

Space Group
P 31 2 1  
Unit Cell

a=99.97Å, b=99.97Å, c=127.37Å
α=90.00, β=90.00, γ=120.00 
Solvent content
52.11  
Matthews coefficient
2.57  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
32.72-2.61Å (2.67-2.61Å)  
Rall(%)
17.8 
Rwork(%)
17.5 (23.0) 
Rfree(%)
24.2 (35.1) 
Num. observed reflections
22934 (1656) 
Num. Rfree reflections
1169 (98) 
Completeness(%)
99.7 (99.2) 

Model parameters

Num Atoms
5176  
Num Waters
218  
Num Hetatoms
0  
Model mean isotropic B factor
44.618Å2  
RMSD bond length
0.017Å  
RMSD bond angle
1.606°  
Filename uploaded
3eev.pdb (uploaded on Oct 28, 2008 1:05 PM)  
Inserted
Oct 28, 2008