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. The active site patch is formed between the two beta sheets, one each from the middle domain and the the C-terminal domain.  

Functional assignment

 

Structure information

Unit cell parameters

Space Group

P 21 21 21  

Unit Cell

a=65.88Å, b=83.19Å, c=128.38Å
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

40.24-2.49Å (2.58-2.49Å)  

R_all(%)

19.7 

R_work(%)

19.1 (22.3) 

R_free(%)

25.6 (33.8) 

Num. observed reflections

26525 (2252) 

Num. R_free reflections

2161 (184) 

Completeness(%)

96.8 (90.0) 

Model parameters

Num Atoms

4755  

Num Waters

234  

Num Hetatoms

234  

Model mean isotropic B factor

44.890Ų  

RMSD bond length

0.012Å  

RMSD bond angle

1.518°  

RMSD dihedral angle

16.891°

 

Filename uploaded

dep.pdb (uploaded on Mar 20, 2011 12:06 AM)  

Inserted

Mar 20, 2011