Journal:Acta Cryst F:S2053230X20011309
From Proteopedia
(Difference between revisions)
| Line 15: | Line 15: | ||
<scene name='85/859611/Cv/21'>Superimposition of MacroD2 crystal structures</scene>: MacroD2-ADPr complex structure (PDB ID [[4iqy]]; (orange) and ligand-free MacroD2 (PDB ID [[6y4y]]) (light blue). ADPr and its surrounding residues are shown as sticks. The labelled residues are important for the catalytic activity of the enzyme. The hydrogen bonds are presented as dash lines. Wa is the catalytic water molecule in MacroD2-ADPr complex. | <scene name='85/859611/Cv/21'>Superimposition of MacroD2 crystal structures</scene>: MacroD2-ADPr complex structure (PDB ID [[4iqy]]; (orange) and ligand-free MacroD2 (PDB ID [[6y4y]]) (light blue). ADPr and its surrounding residues are shown as sticks. The labelled residues are important for the catalytic activity of the enzyme. The hydrogen bonds are presented as dash lines. Wa is the catalytic water molecule in MacroD2-ADPr complex. | ||
| + | |||
| + | Crystal structure comparison of MacroD2 (PDB ID 6Y4Y) and MacroD1 (PDB ID 2X47; (Chen et al, 2011) catalytic fragments showing their mono-ADP-ribosyl-hydrolase functions: | ||
| + | *<scene name='85/859611/Cv/22'>Overall view of the superimposition of apo MacroD2 and MacroD1</scene>. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:12, 31 August 2020
| |||||||||||
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
