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. 2019 Sep 23;63(10):e01202-19. doi: 10.1128/AAC.01202-19

TABLE 1.

Carbapenem complexes of OXA enzymes

Carbapenem Enzyme Source Resolution (Å) Bridge Tautomer PDB accession no.
Imipenem OXA-13 Pseudomonas aeruginosa 1.9 Noa Δ2 1H5X
OXA-23b A. baumannii 1.5 No Δ1R 6N6U
OXA-23c A. baumannii 3.3 No Δ1R 6N6X
OXA-48 K. pneumoniae 1.95 Noa Δ2 5QB4
OXA-48 K. pneumoniae 1.8 Noa Δ2 This work
OXA-239d A. baumannii 1.87 Yes Δ1R 5WIB
Meropenem OXA-13 P. aeruginosa 2.0 Noa Δ2 1H8Y
OXA-23 A. baumannii 2.14 Yes Δ1S 4JF4
OXA-23b A. baumannii 1.5 No Δ1R 6N6V
OXA-23c A. baumannii 3.5 No Δ1R 6N6Y
OXA-48 K. pneumoniae 1.75 Noa Δ2 This work
Ertapenem OXA-48 K. pneumoniae 2.35 Noa Δ2 This work
Doripenem OXA-1 E. coli 1.4 No Δ1R 3ISG
OXA-24/40 A. baumannii 2.25 Yes Δ2 3PAG
OXA-24/40 A. baumannii 2.1 Yes Δ2 3PAE
OXA-48 K. pneumoniae 1.9 Noa Δ2 This work
OXA-51e A. baumannii 1.77 Yes Δ2 5L2F
OXA-239f A. baumannii 1.86 Yes Δ2 5WI7
a

Both OXA-13 and OXA-48 have what is now defined as a pseudobridge rather than the classical hydrophobic bridge seen in the A. baumannii CHDLs.

b

Bridge-deficient mutant, low-pH complex.

c

Bridge-deficient mutant, neutral-pH complex.

d

The imipenem has no tail (truncated at the sulfur) in one molecule in the asymmetric unit.

e

The bridge residues are Phe111 and Trp222.

f

The doripenem is truncated after the pyrrolidine ring in one molecule in the asymmetric unit.