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. Author manuscript; available in PMC: 2009 Dec 11.
Published in final edited form as: Proteins. 2006 Jan 1;62(1):144–151. doi: 10.1002/prot.20702

Fig. 4.

Fig. 4

A comparison of the catalytic site of ykuD with other enzymes. (A) The ykuD catalytic triad with the side-chain of Cys139 rotated to achieve the best stereochemistry; H-bonds are shown by dotted lines, putative oxyanion hole forming backbone amides are denoted by asterisks. (B) Trypsin (PDB entry: 1YYY), with oxyanion hole indicated by asterisks. (C) Comparison of the ykuD and sortase A (PDB entry: 1T2O ) putative Cys-Arg dyads; ykuD residues are shown in light colors and the labels indicating the sortase A amino acids are in italics.