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. 2014 Feb 22;70(Pt 3):760–771. doi: 10.1107/S1399004713033014

Figure 4.

Figure 4

Stereoview of the superposition of ADC-1 (green) and TEM-1 (magenta). Although the polypeptide between ADC-1 helices A4 and A5 (the P2-loop comprising 40 residues unique to the class C enzymes) is substantially longer and is folded completely differently from the corresponding loop between TEM-1 helices H4 and H5 (which comprises only four residues), two residues at the end of the P2-loop (Leu121 and Gln122) occupy the same locations as the two residues at the end of the longer TEM-1 P-loop (Glu104 and Tyr105). The side chain of residue Tyr152, which is critical in the catalytic mechanism of the class C enzymes, is structurally equivalent to the conserved Ser130 side chain in the class A enzymes.