Table 8. Interatomic Distances in Human GlxI Calculated from Molecular Dynamics Simulations (20 ns)^a.

systemb	O2 Gln33	O1 Glu99	His126	Glu172	HO(Oc)	HOH(OHc)
MnA	2.20 ± 0.05	2.11 ± 0.03	2.34 ± 0.07	2.10 ± 0.03	2.17 ± 0.03	2.22 ± 0.05
MnB	2.20 ± 0.05	2.10 ± 0.03	2.36 ± 0.07	2.11 ± 0.03	2.17 ± 0.03	2.22 ± 0.05
CoA	2.20 ± 0.05	2.11 ± 0.05	2.35 ± 0.07	2.11 ± 0.03	2.17 ± 0.03	2.22 ± 0.05
CoB	2.20 ± 0.05	2.09 ± 0.05	2.37 ± 0.08	2.09 ± 0.03	2.17 ± 0.03	2.22 ± 0.09
MgA	2.15 ± 0.05	2.05 ± 0.03	2.32 ± 0.09	2.04 ± 0.03	2.09 ± 0.03	2.15 ± 0.05
MgB	2.15 ± 0.05	2.03 ± 0.03	2.36 ± 0.11	2.04 ± 0.03	2.09 ± 0.03	2.15 ± 0.05
ZnA	2.07 ± 0.04	2.00 ± 0.03	2.21 ± 0.06	1.99 ± 0.03	2.07 ± 0.03	2.10 ± 0.04
ZnB	2.08 ± 0.04	1.99 ± 0.03	2.24 ± 0.08	2.01 ± 0.03	2.07 ± 0.03	2.10 ± 0.04
ZnA,exp65	2.1 (2.0)	2.0 (1.9)	2.0 (2.1)	2.0 (3.3)	2.6(2.1)	2.3 (2.1)
Zne,exp65	1.9 (2.1)	2.0 (1.9)	2.1 (2.1)	2.0 (3.3)	2.8(2.1)	2.2 (2.0)

^aExperimental distances were obtained from the corresponding Zn²⁺–GlxI crystal structure (PDB ID, 1QIP). The zinc ligand distances for the transition state analogue bound-protein structure (PDB ID, 1QIN) are shown in parentheses.^b

^b Subscripts A and B after each metal refer to the relevant active site.

^cIn the HIPC–GSH complex the oxygen atoms of the hydroxycarbamoyl group of the inhibitor replace the two oxygen atoms.