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![[Figure 9]](tz5069fig9mag.jpg)
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Figure 9
(a) Saturation of the Hyp-1 molecules in the two rows, highlighted in blue (I) and pink (II), with ANS ligands. Full occupancy is marked with an x (or 2x if two ligand molecules are found in the general area of a particular binding site), 0.5 denotes a single case (site R3) of 0.5 occupancy. The docked sites 1, 2 and 3 are highlighted in green. An entry on a grey background with designation of contact sites in adjacent (one or two) Hyp-1 molecules repeats another entry marked x. Symmetry-related protein molecules are indicated with primes. ANS molecules farther than 3.2 Å from a particular protein chain are marked in italics. (b) All of the ANS molecules (sticks) superposed using a common frame of the Cα atoms of the nearest protein molecule (shown in ribbon representation). The intramolecular binding sites 1, 2 and 3 are much more constant than the superficial sites, especially 7 and 8. The ANS molecules are colour-coded by the nearest protein molecules in Fig. 6 ![[link]](../../../../../../logos/arrows/d_arr.gif) (a). |
![[Figure 9]](tz5069fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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