Crystal structure of the disulfide engineered HLA-A0201 molecule devoid of peptide (annealed). Determined by X-ray diffraction at 1.75 Å resolution. Released 25 Mar 2020.
Explore 6TDR in 3D Show helices and sheets RCSB PDB PDBe
6TDR contains 28 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 | 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 | 50-52 | 3 | |
| 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 | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 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 |
| β-strand | 51-52 | 2 | 6 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 6 |
| β-strand | 63-71 | 9 | 6 |
| β-strand | 79-84 | 6 | 7 |
| β-strand | 92-95 | 4 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I antigen | A, C | protein | 276 | Homo sapiens | F6IQS1 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
>6TDR_1 MHC class I antigen (chains A, C) AGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEY WDGETRKVKAHSQTHRVDLGTLRGCYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYD GKDYIALKEDLRSWTAADMCAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETL QRTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDG TFQKWVAVVVPSGQEQRYTCHVQHEGLPKPLTLRWE
>6TDR_2 Beta-2-microglobulin (chains B, D) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection. Anjanappa, R., Garcia-Alai, M., Kopicki, J.D. et al. Nat Commun (2020) 11:1314-1314. DOI 10.1038/s41467-020-14862-4 · PubMed
Other PDB entries of the same protein (UniProt F6IQS1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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