Active site of chymotrypsin complexed with the tripeptide Gly-Ala-Trp (residues 250-252, chain C).
The diagram illustrates the catalytic triad of His 57, Asp 102 and Ser 195, as well as showing the ligand's Trp 252 residue nestling in the highly hydrophobic specificity pocket in the active site of the enzyme. (Symbols described here).
LIGPLOT diagram of a SH2 domain-peptide complex (ligand residues 201-205 of chain B). The peptide is a phosphotyrosine, with the phosphorylated tyrosine shown at the top of the picture with its network of hydrogen bonds to the residues of the SH2 domain of the v-src oncogene product.
A "schematic peptide" LIGPLOT diagram. The molecule shown is an antibody-peptide complex (ligand residues 69-75, chain P). Each peptide residue is shown by a circle at the C-alpha position, and only those sidechains which are involved in hydrogen bonds are depicted.
LIGPLOT diagram of part of the pancreatic trypsin inhibitor (residues 15-22, chain I), in a complex with beat-trypsin. Symbols described here.
LIGPLOT diagram of MHC class 1 complex with sendai virus nucleoprotein (residues 1-9, chain P). Symbols described here.
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