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Figure 3
Best-fit overlay of the Cα positions of SABP2 structures (three structures, light blue C atoms) and HbHNL structures (18 structures, white C atoms) onto the structure of HNL6V (green sticks). (a) The catalytic atoms of the catalytic triad in HNL6V (Oγ of Ser80, Nɛ2 of His235, Oδ2 of Asp207) overlay more closely with the corresponding atoms in the HbHNL structures (Ser80, His235 and Asp207) than with the corresponding atoms in the SABP2 structures (Ser81, His238 and Asp210). (b) The oxyanion-hole amide N atoms of Ile12 and Leu81 in HNL6V overlay more closely with the corresponding atoms in HbHNL (Ile12 and Cys81) than with the corresponding atoms in SABP2 (Ala13 and Leu82). The average distances are listed in Table 5[link]. The side-chain conformations differ at OX2 (Cys81 in HbHNL, Leu82 in SABP2) and HNL6V maintains an HbHNL-like conformation despite the Cys81Leu substitution.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 81| Part 9| September 2025| Pages 398-405
https://doi.org/10.1107/S2053230X25007034
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