4V2X
High resolution structure of the full length tri-modular endo-beta-1, 4-glucanase B (Cel5B) from Bacillus halodurans
Summary for 4V2X
Entry DOI | 10.2210/pdb4v2x/pdb |
Descriptor | ENDO-BETA-1,4-GLUCANASE (CELLULASE B), CALCIUM ION, ACETATE ION, ... (6 entities in total) |
Functional Keywords | hydrolase, tri-modular |
Biological source | BACILLUS HALODURANS |
Total number of polymer chains | 1 |
Total formula weight | 69141.80 |
Authors | Venditto, I.,Santos, H.,Ferreira, L.M.A.,Sakka, K.,Fontes, C.M.G.A.,Najmudin, S. (deposition date: 2014-10-15, release date: 2015-02-25, Last modification date: 2024-01-10) |
Primary citation | Venditto, I.,Najmudin, S.,Luis, A.S.,Ferreira, L.M.,Sakka, K.,Knox, J.P.,Gilbert, H.J.,Fontes, C.M. Family 46 Carbohydrate-Binding Modules Contribute to the Enzymatic Hydrolysis of Xyloglucan and Beta-1,3-1,4-Glucans Through Distinct Mechanisms. J.Biol.Chem., 290:10572-, 2015 Cited by PubMed: 25713075DOI: 10.1074/JBC.M115.637827 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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