8C10
Biochemical and structural characterisation of an alkaline family GH5 cellulase from a shipworm symbiont
Summary for 8C10
| Entry DOI | 10.2210/pdb8c10/pdb |
| Descriptor | GH5 Cellulase, MAGNESIUM ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total) |
| Functional Keywords | gh family 5, shipworm, symbiont, enzymatic hydrolysis., hydrolase |
| Biological source | Teredinibacter waterburyi |
| Total number of polymer chains | 1 |
| Total formula weight | 35612.75 |
| Authors | Leiros, I.,Vaaje-Kolstad, G. (deposition date: 2022-12-19, release date: 2023-04-19, Last modification date: 2024-06-19) |
| Primary citation | Junghare, M.,Manavalan, T.,Fredriksen, L.,Leiros, I.,Altermark, B.,Eijsink, V.G.H.,Vaaje-Kolstad, G. Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara. Biotechnol Biofuels Bioprod, 16:61-61, 2023 Cited by PubMed Abstract: Cellulases play a key role in the enzymatic conversion of plant cell-wall polysaccharides into simple and economically relevant sugars. Thus, the discovery of novel cellulases from exotic biological niches is of great interest as they may present properties that are valuable in the biorefining of lignocellulosic biomass. PubMed: 37016457DOI: 10.1186/s13068-023-02307-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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