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

. 2019 Aug 27;9:12438. doi: 10.1038/s41598-019-48850-6

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

© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

The overall structures of GCA-soaked lsBSH complex. (A) It consists of two tetramers, which are composed of chains A, B, C, D, E, F, G and H. In each lsBSH tetramer, one monomer is in complex with the substrate, GCA (in green), while the remaining monomers are in complex with the product, CA (in orange). (B) The tetramer structure formed by chains E, F, G and H. Each monomer has different color. (C) The superimposition of lsBSH monomers bound to GCA. GCA is in green from chain F and light green from chain A. The monomer of chain A contains the second GCA molecule at the vicinity of the active site. (D) The superimposition of lsBSH monomers bound to CA. CA is in orange from chains B, D, G and H and light orange from chains C and E. (E) The superimposition of lsBSH monomers bound to GCA and CA from chains F and B. The catalytic cysteine residue, Cys2 found in the oxidized form is shown in stick representation.