Validation and correction of Zn–CysxHisy complexes

Touw, W.G.; van Beusekom, B.; Evers, J.M.G.; Vriend, G.; Joosten, R.P.

doi:10.1107/S2059798316013036

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 4
Zn—S^γ distance (top) and S^γ—Zn—S^γ angle (bottom) distributions as a function of the number of cysteines and histidines in ZnCys_xHis_y complexes determined at 1.6 Å resolution or better. The contours of the violin plots are kernel density estimates and the box plots are shown as in Fig. 2

. The light grey background areas show one standard deviation around the refinement targets for the Zn—S^γ distance (2.340 ± 0.020 Å) and the S^γ—Zn—S^γ angle (109.5 ± 3.0°). The difference between the types of ZnCys_xHis_y complexes is significant (see Table 1

). When Zn is coordinated by N^δ in ZnCys₃His₁ complexes, the S^γ—Zn—S^γ angle distribution is somewhat bimodal and partly depends on the rotameric state and backbone conformation of the cysteines.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 72| Part 10| October 2016| Pages 1110-1118

https://doi.org/10.1107/S2059798316013036

Open

access

Follow Acta Cryst. D

Search IUCr Journals		doi		Advanced search
Author		volume	page