Meditope-enabled trastuzumab. Determined by X-ray diffraction at 2.0 Å resolution. Released 9 Oct 2013.
Explore 4HJG in 3D Show helices and sheets RCSB PDB PDBe
4HJG contains 25 α-helices and 52 β-strands across 4 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 | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 3 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-154 | 2 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 6 |
| β-strand | 11-12 | 2 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 45-52 | 8 | 8 |
| β-strand | 57-60 | 4 | 8 |
| β-strand | 65 | 1 | 6 |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 8 |
| α-helix | 101-103 | 3 | |
| β-strand | 110 | 1 | 8 |
| β-strand | 114-116 | 3 | 8 |
| β-strand | 117-118 | 2 | 7 |
| α-helix | 122-123 | 2 | |
| β-strand | 124 | 1 | 9 |
| α-helix | 125-126 | 2 | |
| β-strand | 127-131 | 5 | 10 |
| β-strand | 138-139 | 2 | 10 |
| β-strand | 142-152 | 11 | 10 |
| β-strand | 153 | 1 | 9 |
| β-strand | 158-161 | 4 | 11 |
| α-helix | 162-164 | 3 | |
| β-strand | 166 | 1 | 11 |
| β-strand | 170-172 | 3 | 10 |
| α-helix | 173-175 | 3 | |
| β-strand | 176-177 | 2 | 10 |
| β-strand | 183-192 | 10 | 10 |
| α-helix | 193-195 | 3 | |
| β-strand | 196 | 1 | 12 |
| β-strand | 199 | 1 | 12 |
| β-strand | 202-207 | 6 | 11 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-217 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 21-28 | 8 | 2 |
| β-strand | 34-41 | 8 | 2 |
| α-helix | 43-61 | 19 | |
| β-strand | 64-69 | 6 | 2 |
| α-helix | 70-72 | 3 | |
| β-strand | 74-79 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-16 | 12 | |
| α-helix | 22-34 | 13 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-52 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trastuzumab light chain | A | protein | 214 | Homo sapiens | |
| Trastuzumab heavy chain | B | protein | 223 | Homo sapiens | |
| Immunoglobulin G-binding protein A | H | protein | 55 | Staphylococcus aureus | P0A015 (AlphaFold model) |
| Protein L fragment | E | protein | 65 | Finegoldia magna | Q51918 (AlphaFold model) |
>4HJG_1 Trastuzumab light chain (chains A) DIQMTQSPILLSASVGDRVTITCRASQDVNTAVAWYQQRTNGSPRLLIYSASFLYSGVPS RFSGSRSGTDFTLTISSLQPEDIADYYCQQHYTTPPTFGAGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>4HJG_2 Trastuzumab heavy chain (chains B) EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVRQSPGKGLEWVARIYPTNGYTRY ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAIYYCSRWGGDGFYAMDYWGQGTLVTVSS ASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSS GLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC
>4HJG_3 Immunoglobulin G-binding protein A (chains H) SGSYNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTNVLGEAKKLNESQA
>4HJG_4 Protein L fragment (chains E) SGSEVTIKVNLIFADGKIQTAEFKGTFEEATAEAYRYAALLAKVNGEYTADLEDGGNHMN IKFAG
Identification and grafting of a unique peptide-binding site in the Fab framework of monoclonal antibodies. Donaldson, J.M., Zer, C., Avery, K.N. et al. Proc Natl Acad Sci U S A (2013) 110:17456-17461. DOI 10.1073/pnas.1307309110 · PubMed
Other PDB entries of the same protein (UniProt P0A015 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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