6UGV
Crystal structure of the Fab fragment of anti-TNFa antibody infliximab (Remicade) in a I-centered orthorhombic crystal form, Lot C
Summary for 6UGV
Entry DOI | 10.2210/pdb6ugv/pdb |
Descriptor | Infliximab Fab Heavy Chain, Infliximab Fab Light Chain, MESO-ERYTHRITOL, ... (5 entities in total) |
Functional Keywords | antibody, fab, infliximab, biosimilar, tnfa, immune system |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 96064.55 |
Authors | Lerch, T.F.,Sharpe, P.,Mayclin, S.J.,Edwards, T.E.,Polleck, S.,Rouse, J.C.,Conlan, H.D. (deposition date: 2019-09-26, release date: 2019-11-13, Last modification date: 2024-11-06) |
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 (2.4 Å) |
Structure validation
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