   3.4.22.29 | More |
HRV-C15 2Apro consists of two domains: an N-terminal domain comprising of a four-stranded sheet (bI2, cI, eI2 and fI) and a C-terminal domain made up of a six-stranded beta-barrel (aII, bII1, cII2, dII, eII and fII). The N-terminal domain is linked to the C-terminal domain by a long inter-domain loop (residues 40-56). Within the N-terminal domain, a helical turn (Ala17-Leu19) connects cI to eI2. In the C-terminal domain, an antiparallel beta-hairpin, formed by the bII2 and cII1 strands, is located next to the six-stranded beta-barrel. Furthermore, this beta-hairpin also makes close contacts with residues from the N-terminal domain. Three highly conserved residues, His18, Asp34 and Cys105, found in 2Apro from all enteroviruses, form the active site of HRV-C15 2Apro |
752401 |
