This enzyme’s multiple parallel beta sheets form a helical shape that is called a beta helix.
This highly stable structure, thanks to numerous hydrogen bonds and disulfide bonds between strands, is a common characteristic of enzymes involved in the degradation of pectin.
The interior of the beta helix is hydrophobic.

X-ray crystallography has been used to determine the three-dimensional structure of several PGs in different organisms.
 Fungal PGs from Colletotrichum lupini, Aspergillus aculeatus, and Aspergillus niger (PG1 and PG2) have been crystallized.
The PGs from bacteria like Erwinia carotovora and Bacillus subtilis have also been crystallized.

The active site of Fusarium moniliforme PG comprises six charged amino acid residues: H188, R267, and K269 are involved in substrate binding, D212 (a general acid) is responsible for proton donation to the glycosydic oxygen, and D213 and D191 activate H₂O for a nucleophilic attack.
This enzyme’s multiple parallel beta sheets form a helical shape that is called a beta helix. This highly stable structure, thanks to numerous hydrogen bonds and disulfide bonds between strands, is a common characteristic of enzymes involved in the degradation of pectin. The interior of the beta helix is hydrophobic.
X-ray crystallography has been used to determine the three-dimensional structure of several PGs in different organisms.  Fungal PGs from Colletotrichum lupini, Aspergillus aculeatus, and Aspergillus niger (PG1 and PG2) have been crystallized. The PGs from bacteria like Erwinia carotovora and Bacillus subtilis have also been crystallized.
The active site of Fusarium moniliforme PG comprises six charged amino acid residues: H188, R267, and K269 are involved in substrate binding, D212 (a general acid) is responsible for proton donation to the glycosydic oxygen, and D213 and D191 activate H₂O for a nucleophilic attack.
Polygalacturonase