Crystal structure of the Fab 40G5c in complex with a CD3 epsilon peptide. Determined by X-ray diffraction at 1.65 Å resolution. Released 13 May 2026.
Explore 9T46 in 3D Show helices and sheets RCSB PDB PDBe
9T46 contains 18 α-helices and 47 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 |
|---|---|---|---|
| β-strand | 3-6 | 4 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 2 |
| β-strand | 45-51 | 7 | 2 |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 65 | 1 | 1 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 108-109 | 2 | 2 |
| β-strand | 113-117 | 5 | 2 |
| β-strand | 123 | 1 | 3 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 4 |
| α-helix | 134-136 | 3 | |
| β-strand | 137-138 | 2 | 4 |
| β-strand | 141-151 | 11 | 4 |
| β-strand | 152 | 1 | 3 |
| β-strand | 157-160 | 4 | 5 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 5 |
| β-strand | 169-171 | 3 | 4 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 4 |
| β-strand | 182-191 | 10 | 4 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 5 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 6 |
| β-strand | 10-13 | 4 | 7 |
| β-strand | 19-25 | 7 | 6 |
| β-strand | 30 | 1 | 8 |
| β-strand | 37 | 1 | 8 |
| β-strand | 39-44 | 6 | 7 |
| β-strand | 51-55 | 5 | 7 |
| β-strand | 59-60 | 2 | 7 |
| α-helix | 61 | 1 | |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 76-81 | 6 | 6 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-96 | 7 | 7 |
| β-strand | 102-103 | 2 | 7 |
| β-strand | 107-111 | 5 | 7 |
| β-strand | 116 | 1 | 9 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 10 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 134-144 | 11 | 10 |
| β-strand | 145 | 1 | 9 |
| β-strand | 150-155 | 6 | 11 |
| β-strand | 158-159 | 2 | 11 |
| α-helix | 160 | 1 | |
| β-strand | 164-168 | 5 | 10 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 10 |
| α-helix | 188-192 | 5 | |
| β-strand | 196-202 | 7 | 11 |
| β-strand | 210-215 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-8 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin Fab fragment 40G5c, Heavy Chain | H | protein | 224 | Homo sapiens | |
| Immunoglobulin Fab fragment 40G5c, Light Chain | L | protein | 219 | Homo sapiens | |
| T-cell surface glycoprotein CD3 epsilon chain | P | protein | 10 | Homo sapiens | P07766 (AlphaFold model) |
>9T46_1 Immunoglobulin Fab fragment 40G5c, Heavy Chain (chains H) EVQLVQSGAEVKKPGASVKVSCKASGYTFTNYYIHWVRQAPGQGLEWIGWIYPGDGNTKY NEKFKGRATLTADTSTSTAYLELSSLRSEDTAVYYCARDSYSNYYFDYWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDK
>9T46_2 Immunoglobulin Fab fragment 40G5c, Light Chain (chains L) DIVMTQSPDSLAVSLGERATINCKSSQSLLNSRTRKNYLAWYQQKPGQPPKLLIYWASTR ESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCTQSFILRTFGQGTKVEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>9T46_3 T-cell surface glycoprotein CD3 epsilon chain (chains P) QDGNEEMGGX
Engineering of acidic pH-responsive anti-CD3 binding antibodies. La Sala, G., Kroell, K.B., Pincha, M. et al. MAbs (2026) 18:2658902-2658902. DOI 10.1080/19420862.2026.2658902 · PubMed
Other PDB entries of the same protein (UniProt P07766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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