CryoEM structure of HLA-A2 bound to MAGEA8 (232-241) peptide. Determined by electron microscopy at 3.12 Å resolution. Released 3 May 2023.
Explore 8ESB in 3D Show helices and sheets RCSB PDB PDBe
8ESB contains 8 α-helices and 32 β-strands across 2 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 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-83 | 27 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-125 | 5 | 1 |
| β-strand | 126 | 1 | 2 |
| β-strand | 133 | 1 | 2 |
| α-helix | 138-148 | 11 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 3 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-191 | 6 | 4 |
| β-strand | 198-208 | 11 | 4 |
| β-strand | 209 | 1 | 3 |
| β-strand | 213-219 | 7 | 5 |
| β-strand | 222-223 | 2 | 5 |
| β-strand | 229-230 | 2 | 4 |
| β-strand | 234-235 | 2 | 4 |
| β-strand | 241-250 | 10 | 4 |
| β-strand | 257-263 | 7 | 5 |
| β-strand | 270-272 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 6 |
| β-strand | 6-11 | 6 | 7 |
| α-helix | 14-15 | 2 | |
| β-strand | 21-30 | 10 | 7 |
| β-strand | 31 | 1 | 6 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 44-45 | 2 | 8 |
| β-strand | 50-51 | 2 | 7 |
| β-strand | 55-56 | 2 | 7 |
| β-strand | 62-63 | 2 | 7 |
| β-strand | 66-70 | 5 | 7 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 91-94 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin,HLA class I antigen,MAGE-A8 peptide chimera | A, B, C | protein | 448 | Homo sapiens | Q53Z42 (AlphaFold model) |
>8ESB_1 Beta-2-microglobulin,HLA class I antigen,MAGE-A8 peptide chimera (chains A, B, C) GLYDGREHSVGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDI EVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKW DRDMGGGGSGGGGSGGGGSGGGGSGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRF DSDAASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGTLRGCYNQSEAGSHTVQ RMYGCDVGSDWRFLRGYHQYAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQL RAYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLT WQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP EQKLISEEDLGGEQKLISEEDLHHHHHH
Structural analysis of cancer-relevant TCR-CD3 and peptide-MHC complexes by cryoEM. Saotome, K., Dudgeon, D., Colotti, K. et al. Nat Commun (2023) 14:2401-2401. DOI 10.1038/s41467-023-37532-7 · PubMed
Other PDB entries of the same protein (UniProt Q53Z42 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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