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Structure of IDP04432

Crystal Structure of Acyl-CoA Dehydrogenase complexed with FAD from Bacillus anthracis

Edit deposit information
CSGID target
IDP04432 
PDB Id
3OWA (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 17, 2010 
Release Date
Oct 13, 2010 

Annotation

Description
This protein is an enzyme catalyzing the α,β-dehydrogenation of acyl-CoA thioesters to the corresponding trans 2,3-enoyl CoA-products with concommitant reduction of enzyme-bound FAD. The enzyme consists of three domains, all α-helical N-terminal and C-terminal domains which packed side by side, and a small β-barrel middle domain located opposite end of the N-terminal domain. The FAD molecule bound to the patch formed between the C-terminal and N-terminal domains and is covered by the part of the middle domain. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
FAD biological
FMN biological
P5G PEG crystallization
PEG
GOL
SO4
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 1  
Unit Cell

a=75.61Å, b=98.03Å, c=107.74Å
α=92.80, β=106.63, γ=105.30 
Solvent content
55.07  
Matthews coefficient
2.74  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
50.00-1.97Å (2.02-1.97Å)  
Rall(%)
16.4 
Rwork(%)
16.2 (26.4) 
Rfree(%)
20.2 (28.4) 
Num. observed reflections
195012 (13309) 
Num. Rfree reflections
9750 (672) 
Completeness(%)
96.9 (89.7) 

Model parameters

Num Atoms
21062  
Num Waters
2148  
Num Hetatoms
0  
Model mean isotropic B factor
32.250Å2  
RMSD bond length
0.015Å  
RMSD bond angle
1.423°  
Filename uploaded
dep.pdb (uploaded on Sep 17, 2010 3:06 PM)  
Inserted
Sep 17, 2010