 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
journal menu
![[Figure 3]](rl5204fig3mag.jpg)
|
|
Figure 3
H2O2 binding in Gln143Asn MnSOD. (a, b) Resting-state Gln143Asn and wild-type MnSOD enzymes, overlaid on their respective electrostatic surfaces, with the location of the chain A active-site manganese labelled. All bulk-exposed Lb peroxides trapped in the Gln143Asn enzyme are shown as red sticks. Dimeric and tetrameric interfaces are marked by dashed and solid black lines, respectively. Insets show the pentavalent Mn2+ (grey sphere) and Mn3+ (pink sphere) ions and their primary coordination-sphere ligands in the Gln143Asn and wild-type enzymes, respectively. The middle inset shows the ribbon diagram of the tetrameric Gln143Asn MnSOD, with manganese ions shown as grey spheres. (c) Enlarged view of Lb H2O2 (red stick) on top of the displayed electrostatic surface. (d) All modelled H2O2, the active site (top) and the Tyr34–His30 solvent gate with the resting-state water molecules (blue spheres). (e) Enlarged view of the active site of Gln143Asn, with bound LIG (red sticks) peroxide in the treated structure, and the WAT1 solvent (blue spheres) and Wcav. |
![[Figure 3]](rl5204fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
Open 
access
access
