Table 2.

Structural alignment of active site residues of OXA-10, OXA-23, and OXA-48 [51,52,56,57].

DBL numbering [59]	OXA-10	OXA-23	OXA-48
69	Ala66	Ala78	Ala69
70	Ser67	Ser79	Ser70
73	Lys70CX	Lys82CX	Lys73CX
76	Asn73	Asn85	Asn76
102	: Met99	: Phe110	: Ile102
105	Trp102	Trp113	Trp105
118	Ser115	Ser126	Ser118
120	Val117	Val128	Val120
123	: Phe120	: Tyr131	: Tyr123
124	Gln121	Gln132	Gln124
164	Trp154	Trp165	Trp157
165	Leu155	Leu166	Leu158
216	Lys205	Lys216	Lys208
217	Thr206	Thr217	Thr209
218	Gly207	Gly218	Gly210
219	: PHE208	: TRP219	: TYR211
220	Ser209	: Ala220	Ser212
221	Gly210	Met221	Thr213
225	Glu214	Asp222	Arg214
257	Glu244	. Glu253	. Ser242
260	Leu247	Ala256	Leu247
263	Arg250	Arg259	Arg250

* Amino acids in bold are active site residues. Residues stabilizing the oxyanion cleft of the active region are capitalized, residues connecting the conserved active Ser and Lys residues are italicized, and carboxylated Lys residues are labeled with ‘CX’.