Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme’s active site closure

Table 2 Human FPPS structure models analyzed in this study

PDB ID	Res. (Å)	Bisphosphonate inhibitor^a	Other ligands	Conformational state	Literature reference
2F7M	2.30	-	-	Open	[10]
2F8C	2.20	Zoledronate	Pi	Partially closed	[10]
2F8Z	2.60	Zoledronate	IPP	Fully closed	[10]
1YV5	2.00	Risedronate	Pi	Partially closed	[9]
1ZW5	2.30	Zoledronate	IPP	Fully closed	[9]
3N45	1.88	Zoledronate	Pi, FBS_04^b	Partially closed	[21]
3N46	2.35	Zoledronate	Pi, NOV_980^b	Partially closed	[21]
4DEM	1.85	YS0470	-	Partially closed	[12]
4H5C	2.02	YS0470	Pi	Partially closed	Current report
4H5D	2.02	YS0470	PPi	Fully closed	Current report
4H5E	2.05	YS0470	IPP	Fully closed	Current report

^aAll bisphosphonates are bound with Mg²⁺ ions.
^bAllosteric inhibitors.
Please note that in the PDB structures 1YV5, 1ZW5, and 4DEM, the amino acids are numbered with an offset of 14 compared to the rest of the structures. The C-terminal tail KRRK residues in these structures are thus numbered from 364 to 367.