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Crystal structure of T. brucei farnesyl diphosphate synthase

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

PDB
4RYP
Type
protein
Length
698 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Farnesyl pyrophosphate synthase
UniProt
Q86C09
Pockets
2 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFarnesyl pyrophosphate synthaseprotein35175% helix, 1% strandQ86C09
BFarnesyl pyrophosphate synthaseprotein34776% helix, 1% strandQ86C09

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17900.750.7966empty
28870.740.7873empty

Interfaces

1 interface between chains.

  • A–B · 13 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4RYP · Crystal Structure of T. Brucei Farnesyl Diphosphate Synthase · the same entry in another collection · chain A against A, TM-score 1.00

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