MA2-MART1-HLAA0201. Determined by X-ray diffraction at 2.3 Å resolution. Released 23 Nov 2022.
Explore 7TR4 in 3D Show helices and sheets RCSB PDB PDBe
7TR4 contains 25 α-helices and 76 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 | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-273 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| α-helix | 14-15 | 2 | |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 8 |
| β-strand | 5 | 1 | 9 |
| β-strand | 9-12 | 4 | 10 |
| β-strand | 18-23 | 6 | 9 |
| β-strand | 36-40 | 5 | 10 |
| β-strand | 47-51 | 5 | 10 |
| β-strand | 55-56 | 2 | 10 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 9 |
| β-strand | 72-77 | 6 | 9 |
| α-helix | 82-84 | 3 | |
| β-strand | 87-94 | 8 | 10 |
| β-strand | 97-100 | 4 | 10 |
| β-strand | 101 | 1 | 8 |
| β-strand | 104-108 | 5 | 10 |
| β-strand | 114 | 1 | 11 |
| β-strand | 117-121 | 5 | 12 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-129 | 5 | |
| β-strand | 134-142 | 9 | 12 |
| β-strand | 143 | 1 | 11 |
| β-strand | 148-153 | 6 | 13 |
| β-strand | 157 | 1 | 13 |
| β-strand | 162-164 | 3 | 12 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-169 | 2 | 12 |
| β-strand | 175-182 | 8 | 12 |
| α-helix | 185-190 | 6 | |
| β-strand | 194-200 | 7 | 13 |
| β-strand | 203-209 | 7 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 14 |
| β-strand | 11-12 | 2 | 15 |
| β-strand | 18-25 | 8 | 14 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 16 |
| β-strand | 45-51 | 7 | 16 |
| β-strand | 58-60 | 3 | 16 |
| β-strand | 68-73 | 6 | 14 |
| β-strand | 78-83 | 6 | 14 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 16 |
| β-strand | 108-109 | 2 | 16 |
| β-strand | 113-115 | 3 | 16 |
| β-strand | 116-117 | 2 | 15 |
| β-strand | 123 | 1 | 17 |
| β-strand | 126-130 | 5 | 18 |
| β-strand | 142-151 | 10 | 18 |
| β-strand | 152 | 1 | 17 |
| β-strand | 157-160 | 4 | 19 |
| α-helix | 161-163 | 3 | |
| β-strand | 169-171 | 3 | 18 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 18 |
| β-strand | 182-190 | 9 | 18 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 19 |
| β-strand | 211-216 | 6 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA-A*02:01 | A | protein | 278 | Homo sapiens | A0A140T9X5 |
| Beta-2-microglobulin | B | protein | 98 | Homo sapiens | P61769 (AlphaFold model) |
| Light chain | H | protein | 214 | Homo sapiens | |
| Heavy chain | L | protein | 220 | Homo sapiens | |
| Melanoma antigen recognized by T-cells 1 | P | protein | 10 | Homo sapiens | Q16655 (AlphaFold model) |
>7TR4_1 HLA-A*02:01 (chains A) GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEPSS
>7TR4_2 Beta-2-microglobulin (chains B) QRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWS FYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>7TR4_3 Light chain (chains H) QSELTQPRSVSGSPGQSVTISCTGTDRDVGGQNYVSWYQQHPGKAPKLIIHDVIERSSGV PDRFSGSKSGNTASLTISGLQAEDEADYYCWSPAWPYAVFGTGTDVTVLGQPKAAPSVTL FPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSY LSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTEC
>7TR4_4 Heavy chain (chains L) EVQLLESGGGLVQPGGSLRLSCAASGFTFSTYQMSWVRQAPGKGLEWVSGIVSSGGSTAY ADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAGELLPGYGMDVWGQGTTVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
>7TR4_5 Melanoma antigen recognized by T-cells 1 (chains P) ELAGIGILTV
Facile repurposing of peptide-MHC-restricted antibodies for cancer immunotherapy. Yang, X., Nishimiya, D., Lochte, S. et al. Nat Biotechnol (2023) 41:932-943. DOI 10.1038/s41587-022-01567-w · PubMed
Other PDB entries of the same protein (UniProt A0A140T9X5), best resolution first:
MolViewer shows 7TR4 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.