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. 2013 Mar 22;288(18):12828–12839. doi: 10.1074/jbc.M113.459396

FIGURE 3.

FIGURE 3.

The metal binding site of LPMOs. A, close up view of the PchGH61D in the vicinity of the copper binding site (PDB code 4B5Q). The green Fo − Fc map of the copper atom is contoured at 0.41 e/Å3 (3σ). Cyan-colored residues are coordinated to the copper atom. A glycerol molecule was modeled below the copper atom at the active site, colored in pink (denoted GOL). The bound glycerol molecule is stabilized by His-149, Gln-158, and Tyr-75 (in gray) by hydrogen bonds. B, superposition of the metal binding sites of PchGH61D (PDB code 4B5Q; cyan) with the metal binding sites of NcrPMO-2 (4EIR; green), TauGH61A (3ZUD; pink), and HjeGH61B (2VTC; maroon). The metal ions were modeled as Cu2+ in the first three structures and as Ni2+ in the HjeGH61B structure. C, comparison of the metal binding site of PchGH61D (cyan) with the corresponding non-occupied metal binding sites of SmaCBP21 (2BEM; brown) and EfaCBM33 (4A02; orange).