Journal:Acta Cryst D:S2059798321006628
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Comparison of the substrate binding sites of McAA9A and selected AA9 LPMOs, key residues lining the flat surface of: | Comparison of the substrate binding sites of McAA9A and selected AA9 LPMOs, key residues lining the flat surface of: | ||
| - | *<scene name='88/886512/Cv2/ | + | *<scene name='88/886512/Cv2/4'>McAA9F</scene> (PDB entry [[7ntl]]). |
*<scene name='88/886512/Cv1/3'>TaAA9A</scene> (PDB entry [[2yet]]). | *<scene name='88/886512/Cv1/3'>TaAA9A</scene> (PDB entry [[2yet]]). | ||
*<scene name='88/886512/Cv/15'>LsAA9A</scene> (PDB entry [[5acf]]). | *<scene name='88/886512/Cv/15'>LsAA9A</scene> (PDB entry [[5acf]]). | ||
| - | *<scene name='88/886512/Cv/ | + | *<scene name='88/886512/Cv/19'>CvAA9A in complex with cellohexaose</scene> (PDB entry [[6yde]]). |
Loop regions corresponding to L2, L3, and LC for each protein are colored green, magenta, and cyan, respectively. | Loop regions corresponding to L2, L3, and LC for each protein are colored green, magenta, and cyan, respectively. | ||
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| + | <scene name='88/886512/Cv2/5'>The flat surface of McAA9F</scene>. | ||
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| + | <scene name='88/886512/Cv3/6'>Superposition of McAA9F, TaAA9A, LsAA9A, and CvAA9A</scene>. The key residues lining the flat surface are shown in ball-and-stick representation and are colored: McAA9F in salmon, TaAA9A in lemon chiffon, LsAA9A in yellow, and CvAA9A in hot pink. The other residues are shown as trace and are colored in gainsboro. | ||
The structure further contains a rare <scene name='88/886512/Cv/5'>succinimide</scene> substitution that has not been seen in other LPMOs. | The structure further contains a rare <scene name='88/886512/Cv/5'>succinimide</scene> substitution that has not been seen in other LPMOs. | ||
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| + | '''PDB reference:''' McAA9F, [[7ntl]]. | ||
<b>References</b><br> | <b>References</b><br> | ||
Current revision
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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.
