6UGY
Crystal structure of the Fc fragment of anti-TNFa antibody infliximab (Remicade) in a primative orthorhombic crystal form, Lot C
Summary for 6UGY
Entry DOI | 10.2210/pdb6ugy/pdb |
Descriptor | Remicade Fc, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[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, ZINC ION, ... (5 entities in total) |
Functional Keywords | antibody, biologic, biosimilar, infliximab, remicade, fragment crystallizable, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 1 |
Total formula weight | 30038.82 |
Authors | Mayclin, S.J.,Edwards, T.E. (deposition date: 2019-09-26, release date: 2019-11-13, Last modification date: 2024-10-16) |
Primary citation | Lerch, T.F.,Sharpe, P.,Mayclin, S.J.,Edwards, T.E.,Polleck, S.,Rouse, J.C.,Zou, Q.,Conlon, H.D. Crystal Structures of PF-06438179/GP1111, an Infliximab Biosimilar. BioDrugs, 34:77-87, 2020 Cited by PubMed Abstract: Higher-order structure (HOS) assessment is an important component of biosimilarity evaluations. While established spectroscopic methods are routinely used to characterize structure and evaluate similarity, the addition of X-ray crystallographic analysis to these biophysical methods enables orthogonal elucidation of HOS at higher resolution. PubMed: 31650490DOI: 10.1007/s40259-019-00390-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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