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Figure 9
Powder-diffraction structure of the T6 bovine insulin hexamer. Bovine insulin consists of two chains: A (21 amino acids) shown in blue (a) and B (30 amino acids) shown in purple (b). Chain A contains a disulfide between CysA6 and CysA11 (shown in yellow). The chains are held together by two disulfide bonds (shown in yellow) in order to form a monomer (c). Finally, the T6 hexamer is shown in (d). The Cα trace is viewed down the crystallographic threefold axis. The zinc ions are shown as green spheres. Each of the two independent zinc ions is octahedrally coordinated by three HisB10 side chains (shown in purple). Because both Zn atoms lie on the threefold axis, only one is visible in the figure. This figure was generated using PyMOL (https://www.pymol.org/).

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 69| Part 6| June 2013| Pages 978-990
https://doi.org/10.1107/S0907444913003867
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