 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](hv5335fig3mag.jpg)
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Figure 3
Alternate conformations for the omega loop (a) and Arg351 (b) as stereoviews. The structure of StARD3LBD reported here is shown superimposed with the previously determined structure (PDB entry 1em2; charcoal C atoms). Protein residues, including the A conformation, are shown with C atoms colored lime. The B conformation is shown with C atoms colored orange. Solvent molecules located in the tunnel-like cavity are shown as red spheres inside gray molecular surfaces. (a) Ala338 experiences the largest displacement (6.6 Å for Cβ), moving away from the cavity entrance upon switching from the Ω1-b to the Ω1-a conformation. (b) Hydrogen bonds and salt bridges evident for Arg351 in each of two alternate conformations are indicated with dashed yellow lines and distance measurements (Å). In this panel, portal 2, shown as a molecular surface, comprises residues Pro304, Ile319, Leu328 and Ile353, as well as the main-chain atoms of residues 301–303. Residue 388 is Phe (wild type) in the current structure and selenomethionine in the previously reported structure. For clarity, some residues and solvent molecules are not shown. |
![[Figure 3]](hv5335fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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