Table 4.

Residues within 4 Å of the native S58 and comparison with interacting residues of the docked S58, celecoxib and tryptanthrin.

Compounds	Residues within 4 Å of the docked compounds/bound inhibitor	Binding energy (-kcal/mol)	Polar contacts
1CX2 with bound inhibitor (S58)∗	HIS90, ARG120, GLN192, VAL349, LEU352, SER353, TYR355, TYR385, TRP387, ARG513, ALA516, PHE518, VAL523, GLY526, ALA527, LEU351
S58	GLN192, VAL349, LEU352,SER353, GLY 354, TYR355, LEU359, TYR 385, TRP387, ARG513, ALA516, ILE517, PHE518, VAL523, GLY526, ALA527, LEU531	11.2	HIS90 (flex, 2.7A); ARG513 (flex, 2.6 & 2.2A); SER353 (2.1A)
Celecoxib	HIS90, VAL349, LEU352, SER353, TYR355, TYR385, TRP387, ARG513, ALA516, ILE517, PHE518, VAL523, GLY526, ALA527, LEU531	11.3	HIS90 (flex, 2.6A); TYR355 (flex, 2.9A)
Tryptanthrin	ALA199, PHE200, GLN203, VAL295, TRP387, HIS388, LEU390, LEU391, LEU408, HEME	9.7

^∗The residues in bold font are those associating with the native S58 in the designated binding site that are also associating with the other compounds docked with the protein. The residues in italics are those aside from the ones interacting with the native ligand that are also interacting with the docked compounds. Almost all italicized residues for tryptanthrin indicate that the tryptanthrin must have bound to a different site in the protein.