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) |
Experimental 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
Subscripts A and B after each metal refer to the relevant active site.
In the HIPC–GSH complex the oxygen atoms of the hydroxycarbamoyl group of the inhibitor replace the two oxygen atoms.