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. 2014 May 30;70(Pt 6):1704–1717. doi: 10.1107/S139900471400844X

Figure 4.

Figure 4

The hC5a-A8 C-terminal β-strand extension. Close-up view of the hC5a-­A8 C-terminal region adopting a β-strand structure which extends outside the three-helix bundle core. The formation of a two-stranded antiparallel β-sheet between the C-termini of two hC5a-A8 molecules participates in the packing within hC5a-A8 crystals. The residues involved in stabilizing interactions between the two strands are shown as sticks. The position of the carbohydrate chain protruding from Asn741 in native, glycosylated hC5a is indicated by green stars. Black arrows indicate the direction in which the peptide chain could extend in full-length hC5a.