5X88
A crystal structure of cutinases from Malbranchea cinnamomea
Summary for 5X88
| Entry DOI | 10.2210/pdb5x88/pdb |
| Descriptor | cutinase (2 entities in total) |
| Functional Keywords | cutinase malbranchea cinnamomea lipoidase monomer, hydrolase |
| Biological source | Malbranchea cinnamomea |
| Total number of polymer chains | 1 |
| Total formula weight | 21201.76 |
| Authors | Jiang, Z.,Yang, S.Q.,You, X.,Huang, P.,Ma, J.W. (deposition date: 2017-03-01, release date: 2018-01-31, Last modification date: 2024-10-23) |
| Primary citation | Duan, X.,Liu, Y.,You, X.,Jiang, Z.,Yang, S.,Yang, S. High-level expression and characterization of a novel cutinase from Malbranchea cinnamomea suitable for butyl butyrate production. Biotechnol Biofuels, 10:223-223, 2017 Cited by PubMed Abstract: Butyl butyrate has been considered as a promising fuel source because it is a kind of natural ester which can be converted from renewable and sustainable lignocellulosic biomass. Compared with the conventional chemical methods for butyl butyrate production, the enzymatic approach has been demonstrated to be more attractive, mainly owing to the mild reaction conditions, high specificity, low energy consumption, and environmental friendliness. Cutinases play an important role in the butyl butyrate production process. However, the production level of cutinases is still relatively low. Thus, to identify novel cutinases suitable for butyl butyrate synthesis and enhance their yields is of great value in biofuel industry. PubMed: 28932264DOI: 10.1186/s13068-017-0912-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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