TGFB1 in complex with NIS793 FAB. Determined by X-ray diffraction at 2.75 Å resolution. Released 17 Jun 2026.
Explore 13FJ in 3D Show helices and sheets RCSB PDB PDBe
13FJ contains 33 α-helices and 108 β-strands across 6 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 | 281 | 1 | 1 |
| α-helix | 282-286 | 5 | |
| β-strand | 294-296 | 3 | 2 |
| β-strand | 299-301 | 3 | 3 |
| α-helix | 302-306 | 5 | |
| β-strand | 311-313 | 3 | 1 |
| β-strand | 316-318 | 3 | 3 |
| β-strand | 321-323 | 3 | 2 |
| β-strand | 332 | 1 | 1 |
| α-helix | 335-346 | 12 | |
| β-strand | 356-370 | 15 | 1 |
| β-strand | 373-389 | 17 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 7 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 46-51 | 6 | 8 |
| β-strand | 58-60 | 3 | 8 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 7 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 8 |
| β-strand | 108-111 | 4 | 8 |
| β-strand | 115-119 | 5 | 8 |
| α-helix | 123-124 | 2 | |
| β-strand | 125 | 1 | 9 |
| β-strand | 128-132 | 5 | 10 |
| β-strand | 143-153 | 11 | 10 |
| β-strand | 154 | 1 | 9 |
| β-strand | 159-162 | 4 | 11 |
| β-strand | 167 | 1 | 11 |
| β-strand | 171-173 | 3 | 10 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 10 |
| β-strand | 184-193 | 10 | 10 |
| α-helix | 194-197 | 4 | |
| β-strand | 203-208 | 6 | 11 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 12 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 13 |
| β-strand | 18-25 | 8 | 12 |
| β-strand | 34-39 | 6 | 13 |
| β-strand | 46-51 | 6 | 13 |
| β-strand | 58-60 | 3 | 13 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 12 |
| β-strand | 78-83 | 6 | 12 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 13 |
| β-strand | 108-111 | 4 | 13 |
| β-strand | 115-119 | 5 | 13 |
| β-strand | 125 | 1 | 14 |
| β-strand | 128-132 | 5 | 15 |
| β-strand | 143-153 | 11 | 15 |
| β-strand | 154 | 1 | 14 |
| β-strand | 159-162 | 4 | 16 |
| β-strand | 167 | 1 | 16 |
| β-strand | 171-173 | 3 | 15 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 15 |
| β-strand | 184-193 | 10 | 15 |
| α-helix | 194-197 | 4 | |
| β-strand | 203-208 | 6 | 16 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 17 |
| β-strand | 9-12 | 4 | 18 |
| β-strand | 18-23 | 6 | 17 |
| α-helix | 27-29 | 3 | |
| β-strand | 33-37 | 5 | 18 |
| β-strand | 44-47 | 4 | 18 |
| β-strand | 48 | 1 | 19 |
| β-strand | 52 | 1 | 19 |
| β-strand | 61-66 | 6 | 17 |
| β-strand | 69-74 | 6 | 17 |
| α-helix | 79-81 | 3 | |
| β-strand | 84-91 | 8 | 18 |
| β-strand | 96-99 | 4 | 18 |
| β-strand | 103-107 | 5 | 18 |
| α-helix | 110-112 | 3 | |
| β-strand | 113 | 1 | 20 |
| β-strand | 116-120 | 5 | 21 |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| β-strand | 132-141 | 10 | 21 |
| β-strand | 142 | 1 | 20 |
| β-strand | 146-152 | 7 | 22 |
| β-strand | 155-156 | 2 | 22 |
| α-helix | 157 | 1 | |
| β-strand | 161-163 | 3 | 21 |
| α-helix | 164-166 | 3 | |
| β-strand | 167 | 1 | 23 |
| β-strand | 174 | 1 | 21 |
| β-strand | 175 | 1 | 23 |
| β-strand | 176-182 | 7 | 21 |
| α-helix | 184-188 | 5 | |
| β-strand | 193-199 | 7 | 22 |
| β-strand | 202-208 | 7 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 24 |
| β-strand | 9-12 | 4 | 25 |
| β-strand | 18-23 | 6 | 24 |
| α-helix | 27-29 | 3 | |
| β-strand | 33-37 | 5 | 25 |
| β-strand | 44-47 | 4 | 25 |
| β-strand | 48 | 1 | 26 |
| β-strand | 52 | 1 | 26 |
| β-strand | 61-66 | 6 | 24 |
| β-strand | 69-74 | 6 | 24 |
| α-helix | 79-81 | 3 | |
| β-strand | 83-91 | 9 | 25 |
| β-strand | 96-99 | 4 | 25 |
| β-strand | 103-107 | 5 | 25 |
| β-strand | 116-120 | 5 | 27 |
| α-helix | 121-123 | 3 | |
| α-helix | 124-128 | 5 | |
| β-strand | 132-141 | 10 | 27 |
| β-strand | 146-152 | 7 | 28 |
| β-strand | 155-157 | 3 | 28 |
| β-strand | 161-163 | 3 | 27 |
| α-helix | 164-166 | 3 | |
| β-strand | 167-168 | 2 | 27 |
| β-strand | 174-182 | 9 | 27 |
| α-helix | 184-188 | 5 | |
| β-strand | 193-199 | 7 | 28 |
| β-strand | 202-208 | 7 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transforming growth factor beta-1 | A, B | protein | 112 | Homo sapiens | P01137 (AlphaFold model) |
| NIS793 Fab heavy chain | H, I | protein | 224 | Homo sapiens | |
| NIS793 Fab light chain | L, M | protein | 214 | Homo sapiens |
>13FJ_1 Transforming growth factor beta-1 (chains A, B) ALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSK VLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
>13FJ_2 NIS793 Fab heavy chain (chains H, I) QVQLVQSGAEVKKPGSSVKVSCKASGGTFSSYAISWVRQAPGQGLEWMGGIIPIFGTANY AQKFQGRVTITADESTSTAYMELSSLRSEDTAVYYCARGLWEVRALPSVYWGQGTLVTVS SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSC
>13FJ_3 NIS793 Fab light chain (chains L, M) SYELTQPPSVSVAPGQTARITCGANDIGSKSVHWYQQKAGQAPVLVVSEDIIRPSGIPER ISGSNSGNTATLTISRVEAGDEADYYCQVWDRDSDQYVFGTGTKVTVLGQPKAAPSVTLF PPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYL SLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
Biomarker Analysis from Patients with Metastatic PDAC Treated with TGF beta Antibody NIS793 plus Abraxane + Gemcitabine versus Abraxane + Gemcitabine Alone in a Phase II, Open-Label, Randomized Study. Pelletier, M., Yang, J., Joshi, M. et al. Clin Cancer Res (2026) 32:4001-4015. DOI 10.1158/1078-0432.CCR-26-0805 · PubMed
Other PDB entries of the same protein (UniProt P01137 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 13FJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.