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The effects of lysine 200 and phenylalanine 239 farnesyl pyrophosphate synthase (fpps) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates

Analyse The effects of lysine 200 and phenylalanine 239 farnesyl pyrophosphate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NKF
Type
protein
Length
339 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Farnesyl pyrophosphate synthase
EC
2.5.1.10, 2.5.1.1
UniProt
P14324
Ligands
210, MG
Pockets
1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl pyrophosphate synthase (EC 2.5.1.10, 2.5.1.1)protein33976% helix, 1% strandP14324

Ligands and binding sites

  • 210 · Pamidronate · ligand · chains A
  • MG · Magnesium ion · metal · 3 copies · chains A
  • EDO · 1,2-ethanediol · additive · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15000.800.8751MG, 210

Compared structures

  • 4NKF · The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS)… · the same entry in another collection · chain A against A, TM-score 1.00
  • P14324 · AlphaFold monomer V2.0 prediction for farnesyl pyrophosphate synthase (P14324) · a predicted model of the same protein · chain A against A, TM-score 1.00

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