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

. 2012 Aug 28;446(Pt 3):395–404. doi: 10.1042/BJ20120520

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

© 2012 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

(A) Tryptamine was docked into the substrate-binding cavity of the Dat_21–230–AcCoA complex by GOLD [29,50]. The enzyme is shown as a ribbon diagram. The surface electrostatic potential representation of the cavity is shown. Tryptamine is shown as a stick model. Non-polar residues are shown as grey stick models. AcCoA is shown as a ball-and-stick model. Both substrate and cofactor are within the cavity. (B) The catalytic triad residues of Dat. The tryptamine and catalytic triad residues are represented as stick models. AcCoA is shown as a ball-and-stick model. The broken lines identify interactions between the catalytic residues, tryptamine and AcCoA. The numbers represent distance separations between various atoms in angstroms.