Annotation

Description

This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases and participates in d-alanine metabolism and peptidoglycan biosynthesis. The 2.0 A crystal structure of D-alanine--D-alanine ligase from Bacillus anthracis complexed with ATP revealed a dimer with each monomer consisting of three alpha-beta domains. An ATP molecule was found in the active site patch formed between the two beta sheets from the middle domain and the the C-terminal domain. 

Functional assignment

 

Structure information

Unit cell parameters

Space Group

P 1  

Unit Cell

a=56.34Å, b=68.99Å, c=92.39Å
α=73.36, β=84.96, γ=75.46 

Solvent content

 

Matthews coefficient

 

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

32.78-2.00Å (2.03-2.00Å)  

R_all(%)

17.9 

R_work(%)

17.7 (31.8) 

R_free(%)

22.1 (36.0) 

Num. observed reflections

88326 (2493) 

Num. R_free reflections

4451 (124) 

Completeness(%)

96.8 (86.0) 

Model parameters

Num Atoms

9489  

Num Waters

750  

Num Hetatoms

890  

Model mean isotropic B factor

59.190Ų  

RMSD bond length

0.010Å  

RMSD bond angle

1.284°  

RMSD dihedral angle

16.867°

 

Filename uploaded

dep.pdb (uploaded on Mar 20, 2011 3:41 PM)  

Inserted

Mar 20, 2011