HLA-A*0201 single chain trimer with HPV.16 E7 peptide LLMGTLGIV. Determined by X-ray diffraction at 2.22 Å resolution. Released 22 Aug 2018.
Explore 6APN in 3D Show helices and sheets RCSB PDB PDBe
6APN contains 30 α-helices and 60 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 |
|---|---|---|---|
| α-helix | 7-9 | 3 | |
| β-strand | 27 | 1 | 1 |
| α-helix | 28-29 | 2 | |
| β-strand | 30-35 | 6 | 2 |
| β-strand | 45-54 | 10 | 2 |
| β-strand | 55 | 1 | 1 |
| β-strand | 60-65 | 6 | 3 |
| β-strand | 68-69 | 2 | 3 |
| α-helix | 70 | 1 | |
| β-strand | 74-75 | 2 | 2 |
| α-helix | 76-78 | 3 | |
| β-strand | 79-80 | 2 | 2 |
| β-strand | 86-94 | 9 | 2 |
| β-strand | 102-107 | 6 | 3 |
| β-strand | 115-118 | 4 | 3 |
| β-strand | 146-155 | 10 | 4 |
| α-helix | 163 | 1 | |
| β-strand | 164-171 | 8 | 4 |
| β-strand | 174-180 | 7 | 4 |
| β-strand | 189-190 | 2 | 4 |
| α-helix | 193-197 | 5 | |
| α-helix | 200-227 | 28 | |
| β-strand | 237-246 | 10 | 4 |
| β-strand | 252-261 | 10 | 4 |
| β-strand | 264-269 | 6 | 4 |
| β-strand | 276-278 | 3 | 4 |
| α-helix | 281-292 | 12 | |
| α-helix | 295-301 | 7 | |
| α-helix | 302-306 | 5 | |
| α-helix | 307-317 | 11 | |
| α-helix | 319-322 | 4 | |
| β-strand | 326 | 1 | 5 |
| α-helix | 327-328 | 2 | |
| β-strand | 329-335 | 7 | 6 |
| β-strand | 341-351 | 11 | 6 |
| β-strand | 352 | 1 | 5 |
| β-strand | 357-362 | 6 | 7 |
| β-strand | 365-367 | 3 | 7 |
| β-strand | 372-373 | 2 | 6 |
| α-helix | 374-376 | 3 | |
| β-strand | 377-378 | 2 | 6 |
| β-strand | 384-393 | 10 | 6 |
| α-helix | 397-399 | 3 | |
| β-strand | 400-405 | 6 | 7 |
| β-strand | 413-415 | 3 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| β-strand | 27 | 1 | 8 |
| α-helix | 28-29 | 2 | |
| β-strand | 30-35 | 6 | 9 |
| β-strand | 45-54 | 10 | 9 |
| β-strand | 55 | 1 | 8 |
| β-strand | 60-65 | 6 | 10 |
| β-strand | 68-69 | 2 | 10 |
| α-helix | 70 | 1 | |
| β-strand | 74-75 | 2 | 9 |
| β-strand | 79-80 | 2 | 9 |
| β-strand | 86-94 | 9 | 9 |
| β-strand | 102-107 | 6 | 10 |
| β-strand | 115-118 | 4 | 10 |
| α-helix | 119-120 | 2 | |
| β-strand | 146-155 | 10 | 11 |
| α-helix | 163 | 1 | |
| β-strand | 164-171 | 8 | 11 |
| β-strand | 174-180 | 7 | 11 |
| β-strand | 189-190 | 2 | 11 |
| α-helix | 193-196 | 4 | |
| α-helix | 200-227 | 28 | |
| β-strand | 237-246 | 10 | 11 |
| β-strand | 252-261 | 10 | 11 |
| β-strand | 264-269 | 6 | 11 |
| β-strand | 276-278 | 3 | 11 |
| α-helix | 281-292 | 12 | |
| α-helix | 295-301 | 7 | |
| α-helix | 302-306 | 5 | |
| α-helix | 307-317 | 11 | |
| α-helix | 319-322 | 4 | |
| β-strand | 326 | 1 | 12 |
| α-helix | 327-328 | 2 | |
| β-strand | 329-335 | 7 | 13 |
| β-strand | 341-351 | 11 | 13 |
| β-strand | 352 | 1 | 12 |
| β-strand | 357-362 | 6 | 14 |
| β-strand | 365-366 | 2 | 14 |
| β-strand | 371-373 | 3 | 13 |
| α-helix | 374-376 | 3 | |
| β-strand | 377-378 | 2 | 13 |
| β-strand | 384-393 | 10 | 13 |
| α-helix | 397-399 | 3 | |
| β-strand | 400-405 | 6 | 14 |
| β-strand | 413-416 | 4 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin--HLA-A*0201--HPV.16 E7 peptide LLMGTLGIV chimera | A, B | protein | 446 | Homo sapiens | P03129 (AlphaFold model), P04439 (AlphaFold model), P61769 (AlphaFold model) |
>6APN_1 Beta-2-microglobulin--HLA-A*0201--HPV.16 E7 peptide LLMGTLGIV chimera (chains A, B) LLMGTLGIVGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIE VDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWD RDMGGGGSGGGGSGGGGSGGGGSGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFD SDAASQRMEPRAPWIEQEGPEYWDGETRKVKAHSQTHRVDLGTLRGAYNQSEAGSHTVQR MYGCDVGSDWRFLRGYHQYAYDGKDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLR AYLEGTCVEWLRRYLENGKETLQRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTW QRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEEN LYFQGHHHHHHGLNDIFEAQKIEWHE
Effects of HLA single chain trimer design on peptide presentation and stability. Finton, K.A.K. To be published.
Other PDB entries of the same protein (UniProt P03129 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6APN 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.