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. 2007 Jul;16(7):1368–1378. doi: 10.1110/ps.062738307

Figure 3.

Figure 3.

Structures of three active site mutants of PhyAsr. (A) Cys252Ser; (B) Asp223Asn; (C) Arg258Lys; and (D) least-squares superposition of the Cys252Ser mutant structure (yellow loop) with the apo structure (1U24) (gray loop) previously solved (Chu et al. 2004). The critical active site residues are shown as sticks. Least-squares superposition of the P-loop main-chain atoms (residues 251–259) of the Asp223Asn and Arg258Lys mutants, 1U26, and the 1U24 with P-loop of the Cys252Ser mutant results in RMSDs of 0.13, 0.19, 0.11, and 1.15 Å, respectively. Oxygens are shown in red, nitrogens are shown in blue, and sulfur is shown in yellow. Figure was generated with PyMOL (Delano 2002).