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Structure of S. aureus undecaprenyl diphosphate synthase in complex with fpp and sulfate

Analyse Structure of S. aureus undecaprenyl diphosphate synthase in complex with fpp… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4H8E
Type
protein
Length
235 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Undecaprenyl pyrophosphate synthase
EC
2.5.1.31
UniProt
P60477
Ligands
FPP, MG, SO4
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUndecaprenyl pyrophosphate synthase (EC 2.5.1.31)protein23549% helix, 14% strandP60477

Ligands and binding sites

  • FPP · Farnesyl diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • SO4 · Sulfate ion · ion · 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
12660.760.8939MG, FPP, SO4

Compared structures

  • 4H8E · Structure of S. aureus undecaprenyl diphosphate synthase in complex with FPP and sulfate · the same entry in another collection · chain A against A, TM-score 1.00
  • P60477 · AlphaFold monomer V2.0 prediction for isoprenyl transferase (P60477) · a predicted model of the same protein · chain A against A, TM-score 0.99

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