Cystathionine β-Lyase-Like Protein with Pyridoxal Binding Domain Characterized in Leishmania major by Comparative Sequence Analysis and Homology Modelling

Table 1

Comparison of PLP-binding domain in CBLP (L. major) and CBL (A. thaliana).

Docking Pose	CBPL (Leishmania major)				CBL (PDB I.D.1IBJ) of Arabidopsis thaliana
Entry	Observed				Observed	Experimental
	E_conf	E_place	E_score1	Interactions	Interactions
65	0.0	−35.6	−12.8	Tyr95 (OP2, π-π interaction, arene-cation interaction),; Asp169(N–H),; Ser191(OP3); Lys194(OP3, –CHO)	Gly157(OP1); Met158(OP2); Tyr181 (π-π interaction); Ser 275(OP1),; Thr277(OP1),; Lys278(C=O)^#	Tyr127(Op2)*; Arg129(OP4)*; Gly157(OP3); Met158(OP3); Tyr181 (π-π interactions); Asp-253(N–H); Ser275(OP1); Thr277(OP2); Lys278 (aldimine bond)
79	1.7	−27.6	−12.4	Met72(OP1); Tyr95 (OP2, π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP3),; Lys194(OP3, –CHO)
92	1.6	−25.9	−10.6	Gly71(OP3); Tyr95 (π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP2, OP3),; Lys(OP2, –CHO)
102	1.2	−27.3	−10.7	Gly71(OP2); Tyr95 (π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP1, OP3),; Lys(OP1, –CHO)
106	1.6	−60.1	−13.0	Tyr95 (OP1, π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP2),; Lys(OP2, –CHO)
122	0.6	−32.1	−10.4	Tyr95 (OP1, π-π interaction, arene-cation interaction),; Asp169(N–H)Ser191(OP2),; Lys(OP2, –CHO)
143	0.0	−32.2	−11.0	Tyr95 (OP1, π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP1, OP3); Lys(OP3, –CHO)
154	1.0	−32.5	−10.5	Tyr95 (OP1, π-π interaction, arene-cation interaction),; Asp169(N–H); Ser191(OP1, OP2); Lys(OP1, –CHO)

∗These conserved residues are present on the next chain of the enzyme hence not considered here.
^#Susceptible to undergo an aldimine bond formation.
E_conf: energy of PLP conformation in that particular pose; E_plac: energy of the PLP-protein pose at particular place; E-score: energy scoring functions emphasize favorable hydrophobic, ionic, and hydrogen bond contacts.