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Human farnesyl diphosphate synthase complexed with mg and risedronate

Analyse Human farnesyl diphosphate synthase complexed with mg and risedronate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YV5
Type
protein
Length
336 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Farnesyl pyrophosphate synthetase
EC
2.5.1.10
UniProt
P14324
Ligands
RIS, MG, PO4
Pockets
1 · best druggability 0.79

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl pyrophosphate synthetase (EC 2.5.1.10)protein33675% helix, 1% strandP14324

Ligands and binding sites

  • RIS · 1-hydroxy-2-(3-pyridinyl)ethylidene bis-phosphonic acid · ligand · chains A
  • MG · Magnesium ion · metal · 3 copies · chains A
  • PO4 · Phosphate ion · ion · 2 copies · 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
14900.790.8660MG, PO4, RIS

Compared structures

  • 1YV5 · Human farnesyl diphosphate synthase complexed with Mg and risedronate · 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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