4V1Z
The 3-D structure of the cellobiohydrolase, Cel7A, from Aspergillus fumigatus
Summary for 4V1Z
| Entry DOI | 10.2210/pdb4v1z/pdb |
| Related | 4V20 |
| Descriptor | CELLOBIOHYDROLASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, cellulase, biofuels, carbohydrate-active enzyme, thermal 2 stability |
| Biological source | ASPERGILLUS FUMIGATUS |
| Total number of polymer chains | 1 |
| Total formula weight | 47489.59 |
| Authors | Moroz, O.V.,Maranta, M.,Shaghasi, T.,Harris, P.V.,Wilson, K.S.,Davies, G.J. (deposition date: 2014-10-04, release date: 2015-01-14, Last modification date: 2024-10-16) |
| Primary citation | Moroz, O.V.,Maranta, M.,Shaghasi, T.,Harris, P.V.,Wilson, K.S.,Davies, G.J. The Three-Dimensional Structure of the Cellobiohydrolase Cel7A from Aspergillus Fumigatus at 1.5 A Resolution Acta Crystallogr.,Sect.F, 71:114-, 2015 Cited by PubMed Abstract: The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 Å, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts. PubMed: 25615982DOI: 10.1107/S2053230X14027307 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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