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. Author manuscript; available in PMC: 2011 Oct 1.
Published in final edited form as: Proteins. 2010 Oct;78(13):2738–2744. doi: 10.1002/prot.22799

Figure 2. Hsp90N comparisons.

Figure 2

(A) Superposition of the A (ADP-bound) monomer of Hsp90N (blue; bound ADP in yellow) with the structure of the human Hsp90 N-terminal domain bound to geldanamycin (PDB ID 1YET) (gray; bound geldanamycin not shown). The overall r.m.s.d. of the two domains is 0.79 Å. (B) Superposition of the A (ADP-bound) and B (apo) monomers of Hsp90N. Monomer A is colored blue, and monomer B is colored yellow with the ATP-lid red. The conformation of the ATP-lid in monomer B precludes nucleotide binding, as residues 118–121 would directly overlap with the α- and β-phosphates of ADP.