MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Mar 2023.
Explore 7Z0Q in 3D Show helices and sheets RCSB PDB PDBe
7Z0Q contains 10 α-helices and 32 β-strands across 3 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 | 5-15 | 11 | 1 |
| β-strand | 19-26 | 8 | 1 |
| β-strand | 29-35 | 7 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 48-51 | 4 | |
| β-strand | 53 | 1 | 2 |
| α-helix | 56-76 | 21 | |
| α-helix | 80-82 | 3 | |
| β-strand | 85 | 1 | 3 |
| α-helix | 86-87 | 2 | |
| β-strand | 88-93 | 6 | 4 |
| β-strand | 103-112 | 10 | 4 |
| β-strand | 113 | 1 | 3 |
| β-strand | 118-123 | 6 | 5 |
| β-strand | 126-127 | 2 | 5 |
| β-strand | 133-134 | 2 | 4 |
| β-strand | 138-139 | 2 | 4 |
| β-strand | 145-153 | 9 | 4 |
| β-strand | 161-166 | 6 | 5 |
| β-strand | 174-178 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-18 | 12 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 35-41 | 7 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 54-62 | 9 | |
| α-helix | 65-72 | 8 | |
| α-helix | 74 | 1 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-86 | 6 | |
| β-strand | 95 | 1 | 6 |
| β-strand | 98-103 | 6 | 7 |
| β-strand | 115-122 | 8 | 7 |
| β-strand | 123 | 1 | 6 |
| β-strand | 128-131 | 4 | 8 |
| β-strand | 138 | 1 | 8 |
| β-strand | 144 | 1 | 7 |
| β-strand | 148-149 | 2 | 7 |
| β-strand | 155-159 | 5 | 7 |
| β-strand | 171-176 | 6 | 8 |
| β-strand | 184-188 | 5 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 2 |
| α-helix | 11-15 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class II histocompatibility antigen, DR alpha chain | C | protein | 192 | Homo sapiens | P01903 (AlphaFold model) |
| HLA-DRB1 protein | D | protein | 198 | Homo sapiens | D7RIG5 (AlphaFold model) |
| CLIP peptide | G | protein | 17 | Homo sapiens | P04233 (AlphaFold model) |
>7Z0Q_1 HLA class II histocompatibility antigen, DR alpha chain (chains C) IKEEHVIIQAEFYLNPDQSGEFMFDFDGDEIFHVDMAKKETVWRLEEFGRFASFEAQGAL ANIAVDKANLEIMTKRSNYTPITNVPPEVTVLTNSPVELREPNVLICFIDKFTPPVVNVT WLRNGKPVTTGVSETVFLPREDHLFRKFHYLPFLPSTEDVYDCRVEHWGLDEPLLKHWEF DAPSPLPETTEV
>7Z0Q_2 HLA-DRB1 protein (chains D) DTQPRFLWQGKYKCHFFNGTERVQFLERLFYNQEEFVRFDSDVGEYRAVTELGRPVAESW NSQKDILEDRRGQVDTVCRHNYGVGESFTVQRRVHPEVTVYPAKTQPLQHHNLLVCSVSG FYPGSIEVRWFRNGQEEKAGVVSTGLIQNGDWTFQTLVMLETVPRSGEVYTCQVEHPSVM SPLTVEWRARSESAQSKM
>7Z0Q_3 CLIP peptide (chains G) PVSKMRMATPLLMQAGN
MHC-II dynamics are maintained in HLA-DR allotypes to ensure catalyzed peptide exchange. Abualrous, E.T., Stolzenberg, S., Sticht, J. et al. Nat Chem Biol (2023) 19:1196-1204. DOI 10.1038/s41589-023-01316-3 · PubMed
Other PDB entries of the same protein (UniProt P01903 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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