SJ25C1 Fab in complex with soluble CD19. Determined by electron microscopy at 3.4 Å resolution. Released 15 Feb 2023.
Explore 7URX in 3D Show helices and sheets RCSB PDB PDBe
7URX contains 12 α-helices and 57 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-23 | 2 | |
| β-strand | 24-28 | 5 | 1 |
| β-strand | 34-37 | 4 | 2 |
| β-strand | 50-56 | 7 | 1 |
| β-strand | 59-66 | 8 | 1 |
| β-strand | 71-75 | 5 | 2 |
| β-strand | 80-84 | 5 | 2 |
| β-strand | 93-98 | 6 | 1 |
| β-strand | 108-115 | 8 | 1 |
| β-strand | 120-123 | 4 | 3 |
| β-strand | 155-159 | 5 | 3 |
| β-strand | 164-166 | 3 | 3 |
| α-helix | 170-172 | 3 | |
| β-strand | 187-190 | 4 | 1 |
| β-strand | 196-198 | 3 | 2 |
| β-strand | 212-217 | 6 | 1 |
| β-strand | 223 | 1 | 1 |
| β-strand | 226-230 | 5 | 1 |
| β-strand | 239-242 | 4 | 2 |
| β-strand | 245-248 | 4 | 2 |
| β-strand | 257-262 | 6 | 1 |
| β-strand | 267-274 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-25 | 4 | 9 |
| β-strand | 29-31 | 3 | 10 |
| β-strand | 36-44 | 9 | 9 |
| α-helix | 48-50 | 3 | |
| β-strand | 54-58 | 5 | 10 |
| β-strand | 64-70 | 7 | 10 |
| β-strand | 77-79 | 3 | 10 |
| β-strand | 87-92 | 6 | 9 |
| β-strand | 97-103 | 7 | 9 |
| α-helix | 107-109 | 3 | |
| β-strand | 111-121 | 11 | 10 |
| β-strand | 125-131 | 7 | 10 |
| β-strand | 135-139 | 5 | 10 |
| β-strand | 148-150 | 3 | 11 |
| β-strand | 169-173 | 5 | 11 |
| α-helix | 187-188 | 2 | |
| β-strand | 193 | 1 | 12 |
| α-helix | 194-196 | 3 | |
| β-strand | 197-198 | 2 | 11 |
| β-strand | 204-207 | 4 | 11 |
| β-strand | 208 | 1 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23-25 | 3 | 4 |
| β-strand | 29-32 | 4 | 5 |
| β-strand | 38-44 | 7 | 4 |
| β-strand | 52-57 | 6 | 5 |
| β-strand | 64-68 | 5 | 5 |
| β-strand | 72-73 | 2 | 5 |
| α-helix | 74 | 1 | |
| β-strand | 81-84 | 4 | 4 |
| β-strand | 89-94 | 6 | 4 |
| α-helix | 99-101 | 3 | |
| β-strand | 104-109 | 6 | 5 |
| β-strand | 117 | 1 | 5 |
| β-strand | 121-125 | 5 | 5 |
| α-helix | 126-127 | 2 | |
| β-strand | 135-139 | 5 | 6 |
| α-helix | 140-142 | 3 | |
| α-helix | 143-148 | 6 | |
| β-strand | 150-160 | 11 | 6 |
| β-strand | 166-169 | 4 | 7 |
| β-strand | 170-171 | 2 | 8 |
| β-strand | 174-175 | 2 | 8 |
| β-strand | 180-184 | 5 | 6 |
| β-strand | 194-203 | 10 | 6 |
| α-helix | 204-208 | 5 | |
| β-strand | 212-219 | 8 | 7 |
| β-strand | 222-231 | 10 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| B-lymphocyte antigen CD19 | C | protein | 278 | Homo sapiens | P15391 (AlphaFold model) |
| SJ25C1 Fab light chain | L | protein | 235 | Mus musculus | |
| SJ25C1 Fab heavy chain | H | protein | 252 | Mus musculus |
>7URX_1 B-lymphocyte antigen CD19 (chains C) MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKP FLKLSLGLPGLGIHVSPLAIWLFISNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGE LFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSL NQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMW VMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARP
>7URX_2 SJ25C1 Fab light chain (chains L) MGWSCIILFLVATATGVHSDIELTQSPKFMSTSVGDRVSVTCKASQNVGTNVAWYQQKPG QSPKPLIYSATYRNSGVPDRFTGSGSGTDFTLTITNVQSKDLADYFCQQYNRYPYTSGGG TKLEIKRTRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7URX_3 SJ25C1 Fab heavy chain (chains H) MGWSCIILFLVATATGVHSEVKLQQSGAELVRPGSSVKISCKASGYAFSSYWMNWVKQRP GQGLEWIGQIYPGDGDTNYNGKFKGQATLTADKSSSTAYMQLSGLTSEDSAVYFCARKTI SSVVDFYFDYWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTV SWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVE PKSCHHHHHHHH
CD19 CAR antigen engagement mechanisms and affinity tuning. He, C., Mansilla-Soto, J., Khanra, N. et al. Sci Immunol (2023) 8:eadf1426-eadf1426. DOI 10.1126/sciimmunol.adf1426 · PubMed
Other PDB entries of the same protein (UniProt P15391 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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