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![[Figure 2]](gi5011fig2mag.jpg)
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Figure 2
The structure and assembly of human native ALAD. (a) The A monomer of the enzyme (helices coloured pale red and strands light green) looking along the TIM-barrel axis with the large flap covering the active site facing towards the viewer. The catalytic lysine residues, 199 and 252, are shown in ball-and-stick representation. (b) The asymmetric unit of the structure contains a dimer, the second monomer of which (monomer B) is less well defined and is shown at the top in this view (helices cream and strands blue). It can be seen that the large flap covering the active site of monomer B is not defined. (c) The assembly of the complete ALAD octamer with the A and B subunits coloured as in (a) and (b). The active-site zinc ions which are present in the A monomers are indicated as grey spheres. |
![[Figure 2]](gi5011fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
