7VT9
CRYSTAL STRUCTURE AT 3.4 ANGSTROMS RESOLUTION OF Maltodextrin glucosidase, MalZ, FROM Escherichia coli
Summary for 7VT9
Entry DOI | 10.2210/pdb7vt9/pdb |
Descriptor | Maltodextrin glucosidase (2 entities in total) |
Functional Keywords | alpha-amylase, maltodextrin glucosidase, hydrolase |
Biological source | Escherichia coli (strain K12) |
Total number of polymer chains | 2 |
Total formula weight | 140812.39 |
Authors | Ahn, W.-C.,Ahn, Y.,Woo, E.-J. (deposition date: 2021-10-28, release date: 2022-10-26, Last modification date: 2023-11-29) |
Primary citation | Ahn, W.C.,An, Y.,Song, K.M.,Park, K.H.,Lee, S.J.,Oh, B.H.,Park, J.T.,Woo, E.J. Dimeric architecture of maltodextrin glucosidase (MalZ) provides insights into the substrate recognition and hydrolysis mechanism. Biochem.Biophys.Res.Commun., 586:49-54, 2022 Cited by PubMed: 34826700DOI: 10.1016/j.bbrc.2021.11.070 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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