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T. brucei farnesyl pyrophosphate synthase (FPPS)

Analyse T. brucei farnesyl pyrophosphate synthase (FPPS) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R36
Type
protein
Length
324 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.67
Source
Trypanosoma brucei
Molecule
Farnesyl pyrophosphate synthase
UniProt
Q86C09
Pockets
2 · best druggability 0.66

Structure

x-ray diffraction · resolution 1.67 · 1 distinct chain · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl pyrophosphate synthaseprotein32481% helix, 0% strandQ86C09

Ligands and binding sites

  • DMS · Dimethyl sulfoxide · additive · 2 copies · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15460.660.7750DMS
2580.310.7510empty

Compared structures

  • 6R36 · T. brucei farnesyl pyrophosphate synthase (fpps) · the same entry in another collection · chain A against A, TM-score 1.00

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