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. Author manuscript; available in PMC: 2010 Jun 1.
Published in final edited form as: Nat Chem. 2009 Dec 1;1(9):711–715. doi: 10.1038/nchem.412

Figure 2. The position of D112 shifts among the proteins, leading to variations in hydrogen bonding to the carboxylate.

Figure 2

Secondary coordination spheres of Cu(II) in C112D (a, 1.9 Å, PDBID: 3FQY), C112D/M121L (b, 2.1 Å, PDBID: 3FPY), C112D/M121F (c, 1.9 Å, PDBID: 3FQ2), and C112D/M121I (d, 1.9 Å, PDBID: 3FQ1) azurins are highlighted with bond distances shown in Å for heteroatoms involved in the hydrogen bonding “rack” network of the wild-type protein. Oxygen atoms are red; nitrogen atoms are blue.