Class I MHC (HLA-A*02) presenting alpha fetoprotein peptide (AFP). Determined by X-ray diffraction at 2.82 Å resolution. Released 27 Jul 2022.
Explore 7RE8 in 3D Show helices and sheets RCSB PDB PDBe
7RE8 contains 26 α-helices and 60 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 | 4-13 | 10 | 1 |
| α-helix | 21 | 1 | |
| β-strand | 22-29 | 8 | 1 |
| β-strand | 32-38 | 7 | 1 |
| β-strand | 47-48 | 2 | 1 |
| α-helix | 58-85 | 28 | |
| β-strand | 95-104 | 10 | 1 |
| β-strand | 110-119 | 10 | 1 |
| β-strand | 122-127 | 6 | 1 |
| β-strand | 134-136 | 3 | 1 |
| α-helix | 139-150 | 12 | |
| α-helix | 153-159 | 7 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-175 | 11 | |
| α-helix | 177-180 | 4 | |
| β-strand | 184 | 1 | 2 |
| α-helix | 185-186 | 2 | |
| β-strand | 187-193 | 7 | 3 |
| β-strand | 199-209 | 11 | 3 |
| β-strand | 210 | 1 | 2 |
| β-strand | 214-220 | 7 | 4 |
| β-strand | 223-224 | 2 | 4 |
| α-helix | 226-228 | 3 | |
| β-strand | 229-231 | 3 | 3 |
| β-strand | 235-236 | 2 | 3 |
| β-strand | 242-251 | 10 | 3 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-264 | 7 | 4 |
| β-strand | 271-274 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 5 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 6 |
| β-strand | 22-31 | 10 | 6 |
| β-strand | 32 | 1 | 5 |
| β-strand | 37-42 | 6 | 7 |
| β-strand | 45-46 | 2 | 7 |
| α-helix | 47 | 1 | |
| β-strand | 51-52 | 2 | 6 |
| β-strand | 56-57 | 2 | 6 |
| β-strand | 63-71 | 9 | 6 |
| β-strand | 79-84 | 6 | 7 |
| α-helix | 91 | 1 | |
| β-strand | 92-95 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-13 | 10 | 8 |
| α-helix | 21 | 1 | |
| β-strand | 22-29 | 8 | 8 |
| β-strand | 32-38 | 7 | 8 |
| β-strand | 47-48 | 2 | 8 |
| α-helix | 58-85 | 28 | |
| β-strand | 95-104 | 10 | 8 |
| β-strand | 110-119 | 10 | 8 |
| β-strand | 122-127 | 6 | 8 |
| β-strand | 134-136 | 3 | 8 |
| α-helix | 139-150 | 12 | |
| α-helix | 153-159 | 7 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-175 | 11 | |
| α-helix | 177-180 | 4 | |
| β-strand | 184 | 1 | 9 |
| α-helix | 185-186 | 2 | |
| β-strand | 187-193 | 7 | 10 |
| β-strand | 199-209 | 11 | 10 |
| β-strand | 210 | 1 | 9 |
| β-strand | 214-220 | 7 | 11 |
| β-strand | 223-224 | 2 | 11 |
| α-helix | 226-228 | 3 | |
| β-strand | 229-231 | 3 | 10 |
| α-helix | 232-234 | 3 | |
| β-strand | 235-236 | 2 | 10 |
| β-strand | 242-251 | 10 | 10 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-264 | 7 | 11 |
| β-strand | 271-274 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 12 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 13 |
| β-strand | 22-31 | 10 | 13 |
| β-strand | 32 | 1 | 12 |
| β-strand | 36-42 | 7 | 14 |
| β-strand | 45-46 | 2 | 14 |
| α-helix | 47 | 1 | |
| β-strand | 51-52 | 2 | 13 |
| β-strand | 56-57 | 2 | 13 |
| β-strand | 63-71 | 9 | 13 |
| β-strand | 79-85 | 7 | 14 |
| β-strand | 92-95 | 4 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I antigen, A-2 alpha chain | A, D | protein | 276 | Homo sapiens | A0A140T913 (AlphaFold model) |
| Beta-2-microglobulin | B, E | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Phe-met-asn-lys-phe-ile-tyr-glu-ile | C, F | protein | 9 | Homo sapiens | P02771 (AlphaFold model) |
>7RE8_1 MHC class I antigen, A-2 alpha chain (chains A, D) MGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY WDGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD GKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG TFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE
>7RE8_2 Beta-2-microglobulin (chains B, E) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>7RE8_3 PHE-MET-ASN-LYS-PHE-ILE-TYR-GLU-ILE (chains C, F) FMNKFIYEI
Validation and promise of a TCR mimic antibody for cancer immunotherapy of hepatocellular carcinoma. Liu, C., Liu, H., Dasgupta, M. et al. Sci Rep (2022) 12:12068-12068. DOI 10.1038/s41598-022-15946-5 · PubMed
Other PDB entries of the same protein (UniProt A0A140T913 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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