 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](hv5090fig3mag.jpg)
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Figure 3
Binding mode of the aminothiazole ligand to E. coli KAS I protein. (a) Electron density of the aminothiazole ligand (green) bound to the active site of E. coli KAS I protein (grey). The 2Fo − Fc OMIT map (contoured at 1σ) is shown in black; the Fo − Fc OMIT map (contoured at 2.5σ) is shown in orange. The OMIT map in the absence of inhibitor was calculated using the final refined model. (b) Superposition of the binding modes for the KAS I ligands thiolactomycin (cyan), cerulenin (gold) and aminothiazole (green). For the representation of the protein, the structure with bound aminothiazole ligand was used. The protein is shown in surface representation, coloured according to atom type (C, grey; N, blue; O, red; S, yellow). Monomer B of the dimer has been removed, as well as side chains Met204 and Val270 of monomer A, to enable insight into the binding pocket. With an intact binding site, only the acetyl moiety of the aminothiazole ligand is exposed to solvent. The isoprenoid tail of thiolactomycin is buried in a hydrophobic pocket and is not visible in this representation. The structure and binding mode of cerulenin was taken from PDB entry 1fj8 (Price et al., 2001  ). |
![[Figure 3]](hv5090fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
