7VMT
Crystal structure of murine N-acetylglucosaminyl transferase IVa (GnT-IVa) lectin domain in unliganded form
Summary for 7VMT
Entry DOI | 10.2210/pdb7vmt/pdb |
Descriptor | Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
Functional Keywords | glycosyltransferase, lectin, glcnac transferase, posttranslational modification, sugar binding protein |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 6 |
Total formula weight | 99998.10 |
Authors | Nagae, M. (deposition date: 2021-10-09, release date: 2022-06-15, Last modification date: 2024-05-29) |
Primary citation | Nagae, M.,Hirata, T.,Tateno, H.,Mishra, S.K.,Manabe, N.,Osada, N.,Tokoro, Y.,Yamaguchi, Y.,Doerksen, R.J.,Shimizu, T.,Kizuka, Y. Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A). Commun Biol, 5:695-695, 2022 Cited by PubMed: 35854001DOI: 10.1038/s42003-022-03661-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95000641903 Å) |
Structure validation
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