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 Sep 26;24(19):3489. doi: 10.3390/molecules24193489

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

© 2019 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 (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Sequence alignment of Atr-III with other snake venom metalloproteinases (SVMPs) from different pit viper species. The sequence of Atr-III is aligned corresponding to those of the following venom proteins: Bothropasin from B. jararaca (AAC61986), Batroxrhagin from the Brazilian B. atrox (KR632593), Jararhagin from B. jararaca (P30431), B. insularis P-III from B. insularis (AAM09693), Leuc-B from B. leucurus (P86092) and Atr-I, a P-I SVMP from the same B. atrox venom (P85420). Amino acid numbering follows that of Atr-III. Residues are denoted if highly homologous (*) or strongly similar (:). The zinc binding motif (HEGNHLGIHHD) and the methionine 168 of the Met-turn region are invariant and are highlighted in blue. Putative N-linked glycosylation site is bold and boxed in yellow. The cysteine residues are bold and highlighted. Disintegrin-like (ECD) sequences are highlighted in green. Gaps (-) were introduced to optimize the sequence identity. a.a., amino acids. Sequences were aligned using the CLUSTAL W Program.