 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](yt5061fig2mag.jpg)
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Figure 2
ANS binding to copy K of Hyp-1. (a) 2Fo − Fc electron density contoured at 1.5σ around the ligands, showing the ANS molecules (red labels). Two ligands are bound in internal chambers (sites 1 and 2) and one in a deep surface pocket (site 3) formed by residues Lys33 and Tyr150. Sites 1, 2 and 3 are occupied in 22, 25 and 13, respectively, of the 28 protein molecules in the asymmetric unit. Dashed lines indicate hydrogen bonds to protein atoms. The ribbon diagram is annotated with numbered secondary-structure elements, with α for helices, β for β-strands and L for loops. (b) A cutaway view of protein molecule K generated with Chimera (Pettersen et al., 2004  ), showing ligand positions relative to the protein surface. |
![[Figure 2]](yt5061fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
