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Literature summary for 1.14.99.53 extracted from
- Structural dynamics of lytic polysaccharide monoxygenases reveals a highly flexible substrate binding region (2019), J. Mol. Graph. Model., 88, 1-10.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacteria | - |
- |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | role of LPMO's structural dynamics during polysaccharide degradation, comparison of multiple LPMO structures. The substrate binding region is highly flexible with significant and sustained micro-scale level conformational changes.The loops on the binding side of the substrate are most mobile, in concert with the dynamic modes influencing the motions during binding. There are dynamic differences between families AA9, AA10, AA11, and AA13 that consist of more than one structure. The patterns of motion in the loop regions among the AA9 structures are distinct from those in the AA10 structures | Bacteria |
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