TABLE 4.
Metal-ligand and metal-substrate distances for mononuclear iron
Distances are provided in Å.
| Enzyme | Substrate | His-181a Nϵ2 | His-186 Nϵ2 | Asp-304 Oδ1 | Asp-304 Oδ2 | S1b | C9 |
|---|---|---|---|---|---|---|---|
| KshAMtbc | 2.2 | 2.1 | 2.5 | 2.1 | 2.1 | ||
| KshAMtb | ADD | 2.4 | 2.6 | 2.4 | 2.4 | 2.6 | 3.9 |
| KshA1 | 1,4-BNC-CoA | 2.2 | 2.3 | 2.5 | 2.3 | 1.8 | 4.1 |
| KshA5 | 1.9 | 2 | 2.4 | 2.2 | 1.6 | ||
| KshA5 | ADD | 2.2 | 2.4 | 2.8 | 2.3 | 2.4 | 6.4 |
| KshA5 | 1,4-BNC-CoA | 2.3 | 2.2 | 2.5 | 2.7 | 1.9 | 5.8 |
a Residues are numbered for KshAMtb. The corresponding residues in KshA1 are His-181, His-186, and Asp-305. In KshA5, they are His-187, His-192, and Asp-311.
b These are solvent species.
c Data are from Ref. 19.