CryoEM structure of HLA-A2 bound to MAGEA4 (230-239) peptide. Determined by electron microscopy at 3.4 Å resolution. Released 3 May 2023.
Explore 8ESA in 3D Show helices and sheets RCSB PDB PDBe
8ESA contains 7 α-helices and 34 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 |
| α-helix | 20-21 | 2 | |
| β-strand | 23-28 | 6 | 1 |
| β-strand | 31-34 | 4 | 1 |
| β-strand | 47 | 1 | 1 |
| α-helix | 57-84 | 28 | |
| 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 | 138-147 | 10 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| β-strand | 183 | 1 | 3 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-190 | 5 | 4 |
| β-strand | 198-208 | 11 | 4 |
| β-strand | 209 | 1 | 3 |
| β-strand | 214-219 | 6 | 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 | 258-262 | 5 | 5 |
| β-strand | 270-272 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 6 |
| β-strand | 6-11 | 6 | 7 |
| β-strand | 21-28 | 8 | 7 |
| β-strand | 31 | 1 | 6 |
| β-strand | 36 | 1 | 8 |
| β-strand | 39-41 | 3 | 9 |
| β-strand | 44-45 | 2 | 9 |
| 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 | 78-82 | 5 | 9 |
| β-strand | 83 | 1 | 8 |
| β-strand | 91-94 | 4 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera | A, B, C | protein | 448 | Homo sapiens | P61769 (AlphaFold model), Q53Z42 (AlphaFold model) |
>8ESA_1 Beta-2-microglobulin,HLA class I antigen,MAGE-A4 peptide chimera (chains A, B, C) GVYDGREHTVGCGGSGGGGSGGGGSIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDI 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 P61769 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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