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![[Figure 6]](qe5002fig6mag.jpg)
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Figure 6
FLEXR models reveal side-chain repositioning in ligand-binding sites that is missing in other models. (a) Tyr215 in the B chain of the 1.45 Å resolution prostaglandin reductase 3 (MGC45594) structure bound to NAP (PDB entry 2c0c). The qFit (b) and deposited (a) models both share the A conformation. (c) FLEXR detects and models a weak conformation (arrow in the Ringer plot) of Tyr215 oriented away from and no longer hydrogen bonding to the ligand. This feature is not present in either the deposited or qFit models. (d) Lys298 in the B chain of the 1.16 Å resoluton Pyrobaculum aerophilum phosphoglucose isomerase structure bound to glucose 6-phosphate (G6Q; PDB entry 1x9i). (e) qFit-no-bb produces two near-identical rotamers. (f) FLEXR detects a minor side-chain conformation (arrow in the inset Ringer plot) which is oriented away from and no longer interacts with the ligand. The deposited 2mFo − DFc maps are contoured at 1.0σ and the mFo − DFc maps are contoured at −2.0σ/2.0σ (a) or −1.5/1.5σ (c, d, e). Dotted lines represent predicted hydrogen bonds. |
![[Figure 6]](qe5002fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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