5HYI
Glycosylated, disulfide-linked Hole-Hole Fc fragment
Summary for 5HYI
Entry DOI | 10.2210/pdb5hyi/pdb |
Related | 5HY9 5HYE 5HYF |
Descriptor | Ig gamma-1 chain C region, 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)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | bispecific antibody fc engineering knob-into-hole, immune system |
Biological source | Homo sapiens (Human) |
Cellular location | Secreted : P01857 |
Total number of polymer chains | 4 |
Total formula weight | 108105.06 |
Authors | Kuglstatter, A.,Stihle, M.,Benz, J. (deposition date: 2016-02-01, release date: 2017-02-01, Last modification date: 2024-01-10) |
Primary citation | Kuglstatter, A.,Stihle, M.,Neumann, C.,Muller, C.,Schaefer, W.,Klein, C.,Benz, J. Structural differences between glycosylated, disulfide-linked heterodimeric Knob-into-Hole Fc fragment and its homodimeric Knob-Knob and Hole-Hole side products. Protein Eng. Des. Sel., 30:649-656, 2017 Cited by PubMed: 28985438DOI: 10.1093/protein/gzx041 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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