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MolNFT v1 · #101213 · protein

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

4NKF: “The effects of lysine 200 and phenylalanine 239 farnesyl pyrophosphate synthase (fpps) mutations on the…”. X-ray diffraction, 2 ligands (210, MG), 1 pocket (best druggability 0.80). MolNFT v1 #101213 on GenesisL1: 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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