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Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus brevis atcc 367 complexed with citrate

Analyse Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PKO
Type
protein
Length
641 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Geranylgeranyl pyrophosphate synthase
UniProt
Q03Q08
Pockets
5 · best druggability 0.77

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AGeranylgeranyl pyrophosphate synthaseprotein33174% helix, 1% strandQ03Q08
BGeranylgeranyl pyrophosphate synthaseprotein31077% helix, 0% strandQ03Q08

Ligands and binding sites

  • CIT · Citric acid · additive · chains A
  • GOL · Glycerol · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16440.770.8358CIT
26580.720.7965empty
3530.630.9421empty
4630.310.7517empty
5520.290.7510empty

Interfaces

1 interface between chains.

  • A–B · 2030 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 3PKO · Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus brevis atcc… · the same entry in another collection · chain A against A, TM-score 1.00

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