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Table 4 The impact of mutation of interacting residues on p37-p97 binding affinity

From: In silico prediction, characterization, docking studies and molecular dynamics simulation of human p97 in complex with p37 cofactor

The effect of mutation on binding affinity

Interacting residues of p37 UBX domain

Predicted affinity change (ΔΔG affinity)

Binding affinity

PHE(304)-ALA

-0.732 kcal/mol

Decreasing affinity

LEU(269)-ALA

-0.267 kcal/mol

Decreasing affinity

ASN(306)-ALA

-0.446 kcal/mol

Decreasing affinity

LEU(322)-ALA

-0.683 kcal/mol

Decreasing affinity

GLN(260)-ALA

-0.897 kcal/mol

Decreasing affinity

VAL(325)-ALA

-0.582 kcal/mol

Decreasing affinity

ARG(262)-ALA

-1.147 kcal/mol

Decreasing affinity