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. 2022 Jun 7;27(4):397–415. doi: 10.1007/s12192-022-01281-1

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Fig. 2 — Canonical clients bind a conserved, hydrophobic groove in Hsp70’s SBDβ. The SBDβ and lid of DnaK is pictured bound to the model client peptide NRLLLTG (PDB 1DKZ), highlighting the key residues involved. The conservation of those residues across Hsp70 orthologs in E. coli (DnaK), yeast (Ssa1), and humans (mtHsp70, BiP, Hsp72, and Hsc70) is shown from a CLUSTALW multiple sequence alignment