Enzyme Research

Enzyme Research / 2011 / Article / Fig 1

Review Article

Phosphorylcholine Phosphatase: A Peculiar Enzyme of Pseudomonas aeruginosa

Figure 1

Model of PchP. (a) Cartoon representation. The points where loops were eliminated for modeling are indicated by an arrow. (b) A model of PchP representing the pocket detected by ICM-Pro and two conformations of Pcho. Cartoon representation of the secondary structure, stick representation of certain residues and Pcho, and msms (solvent excluded surface) representation of the pocket. Pcho-S: substrate conformation, Pcho-I: inhibitor conformation. (c) Stick representation of residues from the active site of members of the HAD superfamily, plus the hydrophobic pocket surrounding the active site. The residues of the active site are colored by element, and the rest are colored by hydrophobicity according to the Kyte and Doolittle scale [14], in which the most hydrophobic residues are red, and the most hydrophilic are blue.

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