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![[Figure 2]](jc5054fig2mag.jpg)
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Figure 2
The structure of NnGH92 (PDB entry 7nsn). (a) The fold of chain A in ribbon format. The domains are coloured from the N-terminus: CBM-like (white; the fold is split by the first CBM32 insert), CBM32 (lemon), the catalytic domain (ice blue), the second CBM32 (green) and the four-helix bundle (FHB; blue). The linkers between the domains are shown in red and are ordered in the structure. Both mannoimidazoles (ManI) are shown as spheres coloured by atom type: the first at the active site between the two subdomains of the catalytic domain and the second between the catalytic domain and the N-terminal CBM32. The calcium ion adjacent to the active-site ManI is shown as a black sphere. The N-terminal residue (Lys42) and C-terminal residue (Asp1411) are shown as spheres. (b) The surface of the domains coloured as in (a). The extensive packing surfaces of the domains is evident. The ordered linkers between domains are highlighted in red. The images were created with CCP4mg (McNicholas et al., 2011  ). (c) Schematic representation of the domain structure of NnGH92. CBM-like(a) and CBM-like(b) correspond to the same domain structure. |
![[Figure 2]](jc5054fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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