 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](hv5250fig1mag.jpg)
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Figure 1
Ligand binding in the hFPPS–YS0470–2Pi complex. (a) The initial Fourier synthesis map (green mesh, Fo − Fc, contoured at 3σ) showing the electron densities for the bound ligands (sticks) and the metal (yellow spheres) coordinated water molecules (red spheres). The protein surface within 4 Å radius of the bound Pi molecules is shown to indicate the IPP subpocket. (b) An anomalous Fourier map (orange mesh, contoured at 3σ) superimposed onto the structure model. The heights of the anomalous peaks were 4.9, 4.9, 6.1 and 7.8σ for A, B, C and D, respectively. (c) Interactions between the bound ligands, water molecules and the residues of the IPP subpocket. Note that the side chain of Lys57 could not be fully modelled owing to disorder. (d) Secondary-structure elements around the bound ligands. The nomenclature follows that of Tarshis et al. (1994  ). The dipole of the relevant helix is shown. (e) Superposition of the hFPPS–YS0470–2Pi complex and the hFPPS–YS0470–IPP complex (PDB entry 4h5e
, magenta) at the IPP subpocket. The two Pi molecules are outlined in black. Note that Pi1 superposes with the terminal phosphate of IPP (and also with the single Pi bound in the hFPPS–YS0470–Pi complex; not shown). |
![[Figure 1]](hv5250fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
