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Structure of IDP02453

Crystal Structure of Maltose O-Acetyl transferase Complexed with Acetyl Coenzyme A from Bacillus anthracis

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CSGID target
IDP02453  
PDB Id
3IGJ (NCBI MMDB)  
Authors
Maltseva, N., Kim, Y., Papazisi, L., Anderson, W., Joachimiak, A.,CSGID  
Responsible person
Youngchang Kim  
Responsible lab
Argonne National Laboratory  
Deposition Date
2009-07-27  
Release Date
2009-08-04  

Annotation

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Description
This maltose O-acetyltransferase, a member of the hexapeptide-repeat family with a trimeric left-handed parallel beta-helix, transfers an acetyl group from acetyl-CoA to a sugar moiety. In the structure, CoA molecules are located between the two beta-helical chains.  
Functional assignment
 

Ligands

Ligand code Name Ligand type
ACO acetyl coenzyme A biological

Structure information

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Unit cell parameters

Space Group
P 41 21 2  
Unit Cell

a=121.97Å, b=121.97Å, c=142.44Å
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
41.59-2.60Å (2.68-2.60Å)  
Rall(%)
17.5  
Rwork(%)
17.3 (23.1)  
Rfree(%)
21.3 (32.7)  
Num. observed reflections
34815 (2618)  
Num. Rfree reflections
1765 (133)  
Completeness(%)
98.3 (96.0)  

Model parameters

Num Atoms
4731  
Num Waters
176  
Num Hetatoms
310  
Model mean isotropic B factor
52.620Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.437°  
RMSD dihedral angle
20.667°
 
Filename uploaded
dep1w.pdb (uploaded on 2009-07-31 08:36:28-04)