Summary for 6IDW
| Entry DOI | 10.2210/pdb6idw/pdb |
| Related PRD ID | PRD_900005 |
| Descriptor | Glucanase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | orpinomyces sp., gh6, cbh7, endoglucanases, exoglucanases, hydrolase |
| Biological source | Orpinomyces sp. Y102 |
| Total number of polymer chains | 4 |
| Total formula weight | 143951.96 |
| Authors | Tsai, L.C.,Huang, H.C. (deposition date: 2018-09-11, release date: 2018-10-17, Last modification date: 2024-11-06) |
| Primary citation | Huang, H.C.,Qi, L.H.,Chen, Y.C.,Tsai, L.C. Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose. Acta Crystallogr D Struct Biol, 75:1138-1147, 2019 Cited by PubMed Abstract: The catalytic domain (residues 128-449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 Å, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7. PubMed: 31793907DOI: 10.1107/S2059798319013597 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.78 Å) |
Structure validation
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