Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface

Table 3 Structural features of the dimeric interface pocket identified in acetokinase family of enzymes

Protein	PDB code	Identity (%)^a	RMSD (Å²) / C_αaligned^a	Area (Å²)	Volume (Å³)	Reference
St AckA-I-AB	3SLC	100	0 / 797	898	891	present study
St AckA-I-CD	3SLC	100	0.59 / 706	848	866	present study
St AckA-II-AB ^b	3SK3	100	1.44 / 579	-	-	present study
Mt AckA-AB	1G99	43	1.78 / 676	985	1124	[15]
Tm AckA-AB	2IIR	46	1.46 / 764	961	1128	unpublished results
Ma AckA-AB	3P4I	41	1.74 / 708	1114	1088	unpublished results
Ft TdcD-AB	3KHY	45	1.45 / 732	933	1271	unpublished results
St TdcD-AA' ^c	2E1Y	41	1.19 / 744	922	732	[35]
Tm Buk2-AF	1SAZ	16	2.37 / 604	1244	1311	unpublished results ^d

^a Identity and RMSD correspond to the comparison of the query protein with St AckA Form-I dimer (St AckA-I-AB).
^b Due to continuity between the dimeric interface pocket and the active site cavities of A- and B-subunits in Form-II St AckA (Additional file 2: Figure S2C), volume of dimeric interface pocket in Form-II is not well defined.
^cSt TdcD dimer (A' indicates symmetry relation with A) was generated using the crystallographic 2-fold axis.
^d The originally published paper by Diao and Hasson (2009) has been retracted by the publisher for data ownership issues.

ISSN: 1472-6807