Summary for 4XWL
| Entry DOI | 10.2210/pdb4xwl/pdb |
| Related | 4XWM 4XWN |
| Descriptor | Exoglucanase S, DI(HYDROXYETHYL)ETHER, TETRAETHYLENE GLYCOL, ... (10 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Clostridium cellulovorans |
| Total number of polymer chains | 1 |
| Total formula weight | 78610.54 |
| Authors | liaw, Y.-C. (deposition date: 2015-01-29, release date: 2015-10-28, Last modification date: 2023-11-08) |
| Primary citation | Tsai, L.-C.,Amiraslanov, I.,Chen, H.R.,Chen, Y.W.,Lee, H.L.,Liang, P.H.,Liaw, Y.-C. Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage Acta Crystallogr.,Sect.F, 71:1264-1272, 2015 Cited by PubMed Abstract: Exoglucanase/cellobiohydrolase (EC 3.2.1.176) hydrolyzes a β-1,4-glycosidic bond from the reducing end of cellulose and releases cellobiose as the major product. Three complex crystal structures of the glycosyl hydrolase 48 (GH48) cellobiohydrolase S (ExgS) from Clostridium cellulovorans with cellobiose, cellotetraose and triethylene glycol molecules were solved. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme-cellotetraose complex structure, indicating an enzymatic hydrolysis function. Moreover, three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites -2 to -6 in the structure of the ExgS-triethylene glycol complex shown here. Modelling of glucose into subsite -1 in the active site of the ExgS-cellobiose structure revealed that Glu50 acts as a proton donor and Asp222 plays a nucleophilic role. PubMed: 26457517DOI: 10.1107/S2053230X15015915 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.051 Å) |
Structure validation
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