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6WMM

Human poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases

Summary for 6WMM
Entry DOI10.2210/pdb6wmm/pdb
DescriptorN-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, MAGNESIUM ION, ... (8 entities in total)
Functional Keywordsglycosyltransferase, gt-a fold, poly lacnac synthesis, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight88262.53
Authors
Kadirvelraj, R.,Wood, Z.A. (deposition date: 2020-04-21, release date: 2020-12-02, Last modification date: 2021-04-28)
Primary citationKadirvelraj, R.,Yang, J.Y.,Kim, H.W.,Sanders, J.H.,Moremen, K.W.,Wood, Z.A.
Comparison of human poly-N-acetyl-lactosamine synthase structure with GT-A fold glycosyltransferases supports a modular assembly of catalytic subsites.
J.Biol.Chem., 296:100110-100110, 2020
Cited by
PubMed: 33229435
DOI: 10.1074/jbc.RA120.015305
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.548 Å)
Structure validation

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