. 2012 Oct;56(10):5157–5163. doi: 10.1128/AAC.05896-11

Table 2.

Summary of β-lactam docking to NDM-1^a

β-Lactam	Experimentally measured^b		S conformer			I conformer
β-Lactam	K_m (μM)	k_cat/K_m (s⁻¹ μM⁻¹)	Lowest binding energy (kcal/mol)	Estimated K_i (nM)	Population (%)	Lowest binding energy (kcal/mol)	Estimated K_i (nM)	Population (%)
Ampicillin	22	2.2	−12.07	1.4	89	−11.74	2.5	11
Penicillin G	16	3.0	−12.35	0.9	79	−12.53	0.7	21
Piperacillin	12		−12.70	0.5	97	−11.56	3.4	3
Cefepime	77		−11.29	5.3	83	−12.18	1.2	17
Cefotaxime	10		−12.04	1.5	71	−14.23	0.04	29
Cefoxitin	49		−10.61	16.7	51	−12.32	0.9	26
			−12.58^c	0.6^c	4^c	−11.10^d	7.3^d	11^d
						−13.46^e	0.1^e	8^e
Ceftazidime	181		−11.02	8.4	8	−12.7	0.5	86
						−11.25^d	5.7^d	6^d
Cefuroxime	8		−12.06	1.4	45	−12.57	0.6	55
Cephalothin	10		−11.90	1.9	35	−14.30	0.03	62
						−12.02^d	1.5^d	3^d
Faropenem			−12.11	1.3	14	−12.76	0.4	74
						−11.96^d	1.7^d	12^d
Imipenem	94	4.3	−10.39	24.2	62	−11.31	5.2	17
			−10.18^c	34.4^c	7^c	−10.79^d	12.2^d	14^d
Meropenem	49	2.6	−10.64	15.8	84	−11.65	2.9	5
			−11.59^c	3.2^c	11^c
Clavulanic acid	Not detected					−11.44	4.1	100
Aztreonam	Not detected					−12.84	0.4	93
						−12.38^e	0.8^e	7^e
Sulbactam			−10.79	4.7	17	−11.61	3.1	57
						−11.55^d	3.4^d	26^d
Moxalactam						−10.97	9.1	1
						−15.12^f	0.008^f	99^f

In the S conformer, the amide oxygen of the β-lactams interacts with Zn1, while the carboxylic group coordinates with Zn2. The I conformer has the carboxylic or sulfate oxygens interacting with Zn1 and Zn2.

The K_m and k_cat/K_m values are taken from the papers by Yong et al. (38) and by Thomas et al. (28), respectively.

The S2 conformer has switched interactions with the zinc ions from the S conformer.

The I2 conformer has the orientation of the carboxylic group opposite that of I1.

In the I3 conformer, the bridging hydroxide/water is displaced by the carboxylic or sulfate oxygen.

In the I4 conformer, the tyrosyl-carboxylic group chelates with the zinc ions.