8IHY
X-ray crystal structure of Q387E mutant of endo-1,4-beta glucanase from Eisenia fetida
Summary for 8IHY
Entry DOI | 10.2210/pdb8ihy/pdb |
Descriptor | Endoglucanase, MAGNESIUM ION, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | earthworm, cellulase, cold-adapted enzyme, hydrolase |
Biological source | Eisenia fetida (common brandling worm) |
Total number of polymer chains | 1 |
Total formula weight | 51885.53 |
Authors | Kuroki, C.,Hirano, Y.,Nakazawa, M.,Sakamoto, T.,Tamada, T.,Ueda, M. (deposition date: 2023-02-24, release date: 2023-12-06) |
Primary citation | Kuroki, C.,Hirano, Y.,Nakazawa, M.,Sakamoto, T.,Tamada, T.,Ueda, M. A single mutation Asp43Arg was increased 2.5-fold the catalytic activity and maintained the stability of cold-adapted endo-1,4-beta glucanase (Ef-EG2) from Eisenia fetida. Curr Res Biotechnol, 5:-, 2023 Cited by DOI: 10.1016/j.crbiot.2023.100126PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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