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Fig. 8 | BMC Bioinformatics

Fig. 8

From: ppiGReMLIN: a graph mining based detection of conserved structural arrangements in protein-protein interfaces

Fig. 8

Interacting residues at trypsin S1 pocket. The S1 pocket is shown above in the kunitz type trypsin inhibitor complex with porcine trypsin (PDB id 4AN7). The protease surface is depicted in gray with the S1 pocket highlighted in blue. Residue at position S1 from the protease and P1 from the inhibitor are indicated along with ASP189 and GLY193, which are relevant residues as described in literature. Pattern F2 is represented above in the interactions of the P1 residue with ASP189, along with other two neighboring residues. F1 is represented by the interaction of residues in position P1, S1 and GLY193, with the hydrogen bonds from an oxyanion hole depicted in red dashed lines

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