Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Sep 29;12(10):1388. doi: 10.3390/biom12101388

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2022 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

A structure comparison of PW-pGH28-3 and two typical pectinolytic enzymes of Tm_ExoPG and Ec_EndoPG. (A) The predicted structure of PW-pGH28-3. The right-handed parallel β-helix fold is marked with light-grey, and several turns and loops lining the active site cleft are marked with red. (B) The structure of Tm_ExoPG. The right-handed parallel β-helix fold is marked with light-cyan, and several turns and loops lining the active site cleft are marked with green. (C) Superimposition of the predicted PW-pGH28-3 and Tm_ExoPG. (D) The surface structure of PW-pGH28-3. (E) The surface structure of Tm_ExoPG. (F) The surface structure of Ec_EndoPG, which is marked in light-pink. Eight conserved residues in the active site of these three pectinolytic enzymes are all marked in yellow.