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. Author manuscript; available in PMC: 2014 Oct 1.
Published in final edited form as: Mol Immunol. 2013 Mar 29;55(0):212–219. doi: 10.1016/j.molimm.2013.03.002

Figure 5.

Figure 5

Atomic interactions between the side-chain of the polymorphic position 392 in ERAP2. Asn 392 makes hydrogen bonding interactions with Tyr262. Lys392, approaches the N-terminus of the active-site bound lysine amino acid and makes several salt-bridge interactions with catalytically important Glu residues.