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5VU0

Crystal structure of the complex between afucosylated/galactosylated human IgG1 Fc and Fc gamma receptor IIIa (CD16A) with Man5 N-glycans

Summary for 5VU0
Entry DOI10.2210/pdb5vu0/pdb
DescriptorImmunoglobulin gamma-1 heavy chain, Low affinity immunoglobulin gamma Fc region receptor III-A, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
Functional Keywordscomplex, glycosylated, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight73095.36
Authors
Subedi, G.S.,Marcella, A.M.,Barb, A.W. (deposition date: 2017-05-18, release date: 2018-05-23, Last modification date: 2023-10-04)
Primary citationFalconer, D.J.,Subedi, G.P.,Marcella, A.M.,Barb, A.W.
Antibody Fucosylation Lowers the Fc gamma RIIIa/CD16a Affinity by Limiting the Conformations Sampled by the N162-Glycan.
ACS Chem. Biol., 13:2179-2189, 2018
Cited by
PubMed: 30016589
DOI: 10.1021/acschembio.8b00342
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.26 Å)
Structure validation

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