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![[Figure 2]](chr5006fig2mag.jpg)
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Figure 2
Overlay of the catalytic residues of (a) HbHNL (PDB entry 3c6x), (b) HNL40 (PDB entry 8sni) and (c) HNL71 (PDB entry 9clr) onto the esterase SABP2 (PDB entry 1y7h, blue C atoms). The alignment of structures minimized the r.m.s.d. between 205–224 of the 256 corresponding Cα-atom pairs using the align function in PyMOL. The text indicates the structural changes needed for the HNL residues to match the structures of the SABP2 residues. Green text marks changes the improve the match, while red text marks changes that increase the differences. (a) The Cα positions in HbHNL differ by 0.3–1.3 Å from those in SABP2. The OX1 residue shows the largest deviation. The side-chain conformations are similar, except for OX2, which differs by 124° in the χ1 angle. (b) In HNL40, four of the five residues have moved closer to their positions in SABP2, but the serine Cα position and χ1 angle have moved further away. (c) In HNL71 the Cα positions differ by only 0.1–0.4 Å and the χ1 angles differ by less than 7° from those in SABP2. The displacement of the Cα position of the aspartate increases from 0.1 Å in HNL40 to 0.2 Å in HNL71. |
![[Figure 2]](chr5006fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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