 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](rl5206fig4mag.jpg)
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Figure 4
Comparison of the interactions in the active site between MjDHOase and huDHOase (PDB entry 4c6f; Grande-García et al., 2014  ). MjDHOase is in tan and huDHOase is in plum. Labels are in black for MjDHOase and plum for huDHOase. (a) Only interactions involving CA are shown for clarity. CA is at the center. The figure illustrates the high similarity of the active site in the two proteins. (b) Comparison of the interactions of the two residues at the tip of the flexible loop that interact with CA with the protein residues nearby. The figure illustrates the correspondence of some of the interactions and the larger number of interactions in huDHOase compared with MjDHOase (see also Supplementary Table S2). Hydrogen bonds are indicated by dashed lines. Protein residues that make contacts of ≤4.0 Å with these two residues are also shown. The Cα backbones of the two flexible loops are included. Ser143 and Val144 in MjDHOase form one hydrogen bond each (Ser143 OG⋯Asn275 ND2 and Asn89 ND2⋯Val144 8O). Ser143 makes contacts with His168, and Val144 makes contacts with His306. Only one corresponding hydrogen bond is formed in huDHOase (Asn1505 ND2⋯Phe1563 O). However, both Thr1562 and Phe1563 form many contacts. Thr1562 makes contacts with Tyr1558, His1590 and Arg166. Phe1563 makes contacts with His1690, Arg1475, Asn1505, Arg1507 and Pro1701. His1690 (huDHOase) and His306 (MjDHOase) are at corresponding positions and His1590 (huDHOase) and His168 (MjDHOase) are at corresponding positions. |
![[Figure 4]](rl5206fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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