Skip to main content

Table 2 Human FPPS structure models analyzed in this study

From: 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

PDB ID Res. (Å) Bisphosphonate inhibitora 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_04b Partially closed [21]
3N46 2.35 Zoledronate Pi, NOV_980b 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
  1. aAll bisphosphonates are bound with Mg2+ ions.
  2. bAllosteric inhibitors.
  3. 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.