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Structure of IDP01610

X-ray crystal structure of homoserine O-acetyltransferase from Bacillus anthracis.

Edit deposit information
CSGID target
IDP01610 
PDB Id
3I1I (NCBI MMDB
Authors
J.Osipiuk,M.Zhou,S.Grimshaw,W.F.Anderson,A.Joachimiak 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jun 26, 2009 
Release Date
Jul 07, 2009 

Annotation

Description
Homoserine O-acetyltransferases belong to esterase_lipase protein super-family. They catalyze reaction of the transfer of acetyl group from acetyl-CoA to homoserine which is the first part of methionine biosynthesis pathway. This biosynthetic pathway is absent in mammals. Therefore, homoserine O-acetyltransferase is an attractive antimicrobial target. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
ACT
GOL
PO4 PHOSPHATE ION
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 61 2 2  
Unit Cell

a=123.22Å, b=123.22Å, c=295.17Å
α=90.00, β=90.00, γ=120.00 
Solvent content
66.75  
Matthews coefficient
3.7  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
47.30-2.44Å (2.50-2.44Å)  
Rall(%)
16.3 
Rwork(%)
16.1 (21.9) 
Rfree(%)
19.7 (27.4) 
Num. observed reflections
50039 (3557) 
Num. Rfree reflections
2551 (172) 
Completeness(%)
99.4 (97.7) 

Model parameters

Num Atoms
6427  
Num Waters
347  
Num Hetatoms
0  
Model mean isotropic B factor
23.260Å2  
RMSD bond length
0.017Å  
RMSD bond angle
1.487°  
Filename uploaded
idp01610.pdb (uploaded on Jun 26, 2009 6:30 PM)  
Inserted
Jun 26, 2009