Figure 8
![Figure 8](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2F1472-6807-9-9/MediaObjects/12900_2008_Article_229_Fig8_HTML.jpg)
Flexibility in substrate binding at the GAPDH active site (stereo). Position of D-G3H in the CpGAPDH ternary complex subunit A (yellow), subunit D (wheat); mutant BsGAPDH ternary complex (PDBId: 1nqo) subunit O (pale cyan); BsGAPDH thiacyl intermediate (PDBId: 3cmc) subunit O (light green); E. coli GAPDH (1dc4) subunit O (light pink). The 'Ps' and 'new Pi' sites are indicated. A sulfate ion is bound in each subunit of the BsGAPDH complex.