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Crystal structure of human farnesyl pyrophosphate synthase (T201A mutant) complexed with mg and zoledronate

Analyse Crystal structure of human farnesyl pyrophosphate synthase (T201A mutant)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4KFA
Type
protein
Length
338 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
ZOL, MG
Pockets
1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl pyrophosphate synthase (EC 2.5.1.10, 2.5.1.1)protein33875% helix, 1% strandP14324

Ligands and binding sites

  • ZOL · Zoledronic acid · ligand · chains A
  • MG · Magnesium ion · metal · 3 copies · chains A
  • EDO · 1,2-ethanediol · 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
15560.780.8568MG, ZOL

Compared structures

  • 4KFA · Crystal structure of human farnesyl pyrophosphate synthase (t201a mutant) complexed with… · 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 0.99

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