Journal:Acta Cryst D:S205979832100677X
From Proteopedia
(Difference between revisions)
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*<scene name='88/886503/Cv/22'>The dimer formation of WcAG with 180ᴼ rotation</scene>. | *<scene name='88/886503/Cv/22'>The dimer formation of WcAG with 180ᴼ rotation</scene>. | ||
| - | ''Wc''AG formed a <scene name='88/886503/Cv/26'>homodimer, of which the N-terminal domain of one monomer orientated in proximity to the catalytic domain of another</scene>, creating the substrate-binding groove. The residues near the dimer interface are shown in dark blue and deep sky blue sticks, while the maltotriose and catalytic residues are represented by yellow and magenta, respectively. The active site of ''Wc''AG was naturally designed to fit perfectly with maltotriose. The Arg-Glu salt bridge gate (R176-E296) in front of the active site modulates the substrate specificity of ''Wc''AG. | + | ''Wc''AG formed a <scene name='88/886503/Cv/26'>homodimer, of which the N-terminal domain of one monomer orientated in proximity to the catalytic domain of another</scene>, creating the substrate-binding groove. The residues near the dimer interface are shown in dark blue and deep sky blue sticks, while the maltotriose and catalytic residues are represented by yellow and magenta, respectively. The active site of ''Wc''AG was naturally designed to fit perfectly with maltotriose. The Arg-Glu salt bridge gate (R176-E296) in front of the active site modulates the substrate specificity of ''Wc''AG. |
Ligand binding sites: | Ligand binding sites: | ||
Revision as of 14:51, 4 July 2021
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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.
