Skip to main content
. Author manuscript; available in PMC: 2009 Aug 29.
Published in final edited form as: J Mol Biol. 2008 Jun 10;381(2):383–393. doi: 10.1016/j.jmb.2008.06.012

Table 2.

Active site distances in DD-peptidases

Distance (Å)
Enzyme/ligand Asn Cα-Gly Cαa Ser Cα-Gly Cαa
E. coli PBP5 12.7 8.9
E. coli PB5/5 12.5 8.8
E. coli PBP5/6 12.4 8.7
E. coli PBP5/boronate 11.8 8.1
S. pneumoniae PBP3 11.6 8.3
R39 DD-peptidase 11.3 8.1
R39 DD-peptidase/6 10.8 7.8
R39 DD-peptidase/7 11.2 8.2
a

These refer to the Asn and Ser residues of the SXN motif, and the Gly residue of the KXG motif of the respective enzymes