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

. 2015 Oct 1;43(19):9446–9456. doi: 10.1093/nar/gkv989

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

© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 4. — Structural characterization of the human Dus2 domain. (A) The structure of HsDus2^dusD shows the typical (α/β)₈ TIM barrel fold (α helices in green, β strands in yellow) but contains three additional β strands (red). The FMN coenzyme (yellow) lies at the center of the barrel. This domain is directly connected to the α-helical sub-domain (blue). (B) Molecular interface between the TIM barrel and the helical sub-domain. The interface is mainly hydrophobic and stabilized by hydrogen bonds, π−cation interactions (R21-Y283, R290-W247) and one salt-bridge (D33-K276). For clarity, residues belonging to α11, α12 and part of α13 are not displayed. (C) HsDus2 active site showing the molecular interaction between the FMN redox cofactor (yellow) and the residues in its immediate vicinity (green). For simplicity, only the major FMN conformation is displayed.