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. 2020 Aug 19;76(Pt 9):428–437. doi: 10.1107/S2053230X20010250

Figure 2.

Figure 2

Stereoviews of the H82F/F202Y HDAC6 CD1–trichostatin A complex (PDB entry 6wyo). (a) Polder OMIT maps (Liebschner et al., 2017 ▸) showing trichostatin A bound to monomer A (contoured at 3.5σ), Phe82 (contoured at 2.0σ) and Tyr202 (contoured at 2.5σ). Atoms are color-coded as follows: C, light blue (monomer A), light gray (monomer B) or wheat (inhibitor); N, blue; O, red; Zn2+, gray sphere. Metal-coordination and hydrogen-bond interactions are indicated by solid and dashed black lines, respectively. (b) Polder OMIT maps showing trichostatin A bound to monomer B (contoured at 3.5σ), Phe82 (contoured at 2.0σ) and Tyr202 (contoured at 2.5σ). Atoms are color-coded as in (a). (c) Superposition of the trichostatin A complexes with wild-type HDAC6 CD1 (PDB entry 6uo2; monomer B) and H82F/F202Y HDAC6 CD1 (PDB entry 6wyo; monomer A). Residue 82 displays slight flexibility, consistent with the weaker electron density observed for Phe82 in (a) and (b). Atoms are color-coded as follows: C, light blue (H82F/F202Y HDAC6 CD1), light gray (HDAC6 CD1), wheat (trichostatin A bound to H82F/F202Y HDAC6 CD1) or orange (trichostatin A bound to wild-type HDAC6 CD1); N, blue, O, red; Zn2+, gray sphere.