Table 1.

Electrostatic interaction distances between ligand and ODC

Interaction	Ligand ⋯ Enzyme	Distance, Å
		ODC⋅OMP	ODC⋅I−	ODC⋅BMP†
Carboxylate binding	O8 ⋯ Asp-91(Oδ2)	3.49  ± 0.23	4.43  ± 0.83
	O8 ⋯ Asp-96(Oδ1)	4.08  ± 0.30	7.86  ± 0.98
	O8 ⋯ Lys-93(Nζ)	2.70  ± 0.10	5.38  ± 1.33
	C6 ⋯ Asp-91(Oδ2)	5.79  ± 0.22	4.02  ± 0.18	2.82
	C6 ⋯ Asp-96(Oδ1)	5.34  ± 0.27	3.99  ± 0.20	4.24
	C6 ⋯ Lys-93(Nζ)	4.89  ± 0.15	2.82  ± 0.10	2.70
Ribose binding	O2′ ⋯ Lys-59(Nζ)	2.99  ± 0.44	4.48  ± 0.23	4.84
	O3′ ⋯ Lys-59(Nζ)	3.83  ± 0.47	2.87  ± 0.14	3.16
	O3′ ⋯ Ser-35(Oγ)	2.89  ± 0.20	3.45  ± 0.26	3.58
	O3′ ⋯ Asp-37(Oδ2)	6.92  ± 1.48	2.84  ± 0.34	2.86
Phosphate binding	Phosphate O ⋯ Arg-235(Nη2)	2.85  ± 0.35	2.74  ± 0.12	2.84
	Phosphate O ⋯ Arg-235(Nη1)	2.94  ± 0.34	2.90  ± 0.25	2.82
	Phosphate O ⋯ Tyr-217(OH)	2.60  ± 0.09	2.62  ± 0.09	2.68
	Phosphate O ⋯ Gln-215(Nɛ2)	4.30  ± 0.36	3.28  ± 0.60	5.19
Capping loop	O2 ⋯ Gln-215(Nɛ2)	3.23  ± 0.45	3.43  ± 0.39	4.01
	O4 ⋯ Ser-154(N)	2.96  ± 0.20	3.31  ± 0.33	2.78
	O4 ⋯ Ser-154(Oγ)	3.41  ± 0.22	3.97  ± 0.24	3.76
	O4 ⋯ Cys-155(Sγ)	3.56  ± 0.47	6.05  ± 0.49	5.88

^†ODC⋅BMP data are taken from the crystal structure of ref. 9.