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Figure 4
Comparison of hROR1-KRD with structurally related KRDs. (a) Cartoon representation of the superposition of hROR1-KRD with the closest structurally related KRDs from homologous proteins identified by DALI and PDBeFold, as detailed in Supplementary Table S1: PDB entries 5ct3 (cyan), 1i71 (dark blue), 1krn (pink), 2doh (light green), 6rx7 (orange), 1nl2 (brown), 1kiv (light blue), 6oqk (dark green) and 2k51 (red). (b) Details of the nonconserved lysine residue at position 369 in hROR1-KRD (shown in red), occupying a site displaying a negatively charged residue used by HGF/SF (orange), plasminogen (dark blue) and apolipoprotein KRDs (cyan, pink and light blue) to bind lysine and its analogs [aminocaproic acid (ACA) from PDB entry 2pk4 is shown in yellow ball-and-stick representation].

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 78| Part 5| May 2022| Pages 185-192
https://doi.org/10.1107/S2053230X22003855
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