Structure of FabS1CE2_P4a in complex with the N-terminal domain of PD-L1. Determined by X-ray diffraction at 1.64 Å resolution. Released 30 Sept 2026.
Explore 13DT in 3D Show helices and sheets RCSB PDB PDBe
13DT contains 25 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 |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 17-25 | 9 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 3 |
| β-strand | 46-52 | 7 | 3 |
| β-strand | 57-60 | 4 | 3 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-84 | 7 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 3 |
| β-strand | 109-110 | 2 | 3 |
| β-strand | 114-116 | 3 | 3 |
| β-strand | 117-118 | 2 | 2 |
| β-strand | 123 | 1 | 4 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 5 |
| α-helix | 131-133 | 3 | |
| β-strand | 138 | 1 | 5 |
| β-strand | 141-151 | 11 | 5 |
| β-strand | 152 | 1 | 4 |
| β-strand | 157-160 | 4 | 6 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 6 |
| β-strand | 169-171 | 3 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 5 |
| β-strand | 182-191 | 10 | 5 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 6 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-13 | 4 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 33-38 | 6 | 8 |
| β-strand | 45-49 | 5 | 8 |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 7 |
| β-strand | 70-75 | 6 | 7 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 8 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 8 |
| β-strand | 102-106 | 5 | 8 |
| β-strand | 111 | 1 | 9 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 10 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 10 |
| β-strand | 140 | 1 | 9 |
| β-strand | 145-150 | 6 | 11 |
| β-strand | 153-154 | 2 | 11 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 10 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 10 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 11 |
| β-strand | 201-208 | 8 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22 | 1 | 12 |
| β-strand | 27-31 | 5 | 13 |
| β-strand | 36-38 | 3 | 14 |
| β-strand | 41 | 1 | 12 |
| α-helix | 48 | 1 | |
| α-helix | 50-52 | 3 | |
| β-strand | 54-59 | 6 | 13 |
| β-strand | 62-68 | 7 | 13 |
| β-strand | 71-72 | 2 | 13 |
| α-helix | 74-76 | 3 | |
| α-helix | 79-81 | 3 | |
| β-strand | 85-87 | 3 | 14 |
| α-helix | 89-94 | 6 | |
| β-strand | 96 | 1 | 12 |
| β-strand | 99-101 | 3 | 14 |
| α-helix | 106-108 | 3 | |
| β-strand | 110-117 | 8 | 13 |
| β-strand | 121-131 | 11 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FabS1CE2_P4a heavy chain | A | protein | 227 | Homo sapiens | |
| FabS1CE2_P4a light chain (Trastuzumab Fab Light Chain) | B | protein | 217 | Homo sapiens | |
| Programmed cell death 1 ligand 1 | C | protein | 126 | Homo sapiens | Q9NZQ7 (AlphaFold model) |
>13DT_1 FabS1CE2_P4a heavy chain (chains A) EVQLVESGGGLVQPGGSLRLSCAASGFTLENYDIHWVRQAPGKGLEWVAWIYPRNGFTAY ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARLLWYDIHAMDYWGQGTLVTVFN QIQGPSVFPLAPSSKSTSGGTAALGCLVKDYFPGPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
>13DT_2 FabS1CE2_P4a light chain (Trastuzumab Fab Light Chain) (chains B) AAAVADIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQKPGKAPKLLIYSASFLY SGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQHYTTPPTFGQGTKVEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVSWYVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTQGTTSVTKSFNRGEC
>13DT_3 Programmed cell death 1 ligand 1 (chains C) FTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQH SSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNALVPRGS HHHHHH
Water and common crystallization additives (NA, PEG, EDO) are not listed.
Strategy for modular assembly of tetravalent, multispecific antibodies. Mallette, E., Blazer, L.L., Hokanson, C.A. et al. Protein Sci (2026) 35:e70797-e70797. DOI 10.1002/pro.70797 · PubMed
Other PDB entries of the same protein (UniProt Q9NZQ7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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