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. 2017 Nov 14;16:197. doi: 10.1186/s12934-017-0801-y

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — The site mutants selected for site PEGylation modified of Sak. a The five residues of Sak monomer selected for site PEGylation modified, Gly79, Leu82, Lys84, Ala97, and Arg104, were marked with sticks (PDB code 2sak). b Shown is the electrostatic potential surface of the monomer Sak (PDB code 2sak) in the same orientation as in a. c The five residues of Sak (Sak-μPl plasminogen complex) selected for site PEGylation modified, Gly79, Leu82, Lys84, Ala97, and Arg104, were marked with sticks (PDB code 1bui). d Shown is the electrostatic potential surface of Sak-μPl plasminogen complex (PDB code 1bui) in the same orientation as in c. Saturating Red indicates A < − 10 kiloteslase/e, and saturating blue indicates A > 10 kiloteslase/e, T = 293K