Figure 2 | Scientific Reports

Figure 2

From: Structure of polyhydroxyalkanoate (PHA) synthase PhaC from Chromobacterium sp. USM2, producing biodegradable plastics

Figure 2

The catalytic residues of PhaC Cs -CAT. (a) A close-up view of the catalytic site of PhaC Cs -CAT. The catalytic triad residues (orange) comprise Cys291, His477 and Asp447, with a hydrogen bond between His477 and Asp447. The catalytic center Cys291 is located at the nucleophilic elbow sandwiched with nonpolar residues Phe290 and Val292 (green). Hydrogen bonds are indicated by broken lines. (b) Overlay of the catalytic triad of PhaC Cs -CAT (orange) onto human gastric lipase (1HLG in green). (c) Overlay of the active site with the catalytic triad of PhaC Cs -CAT (orange) onto those of PhaC Cn -CAT (5T6O in yellow; 5HZ2 in magenta). The imidazole ring of the His residue of PhaC Cn -CAT (magenta) is flipped from the other two.

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