Crystal structure of H-2Dd with C84-C139 disulfide in complex with gp120 derived peptide P18-I10. Determined by X-ray diffraction at 2.37 Å resolution. Released 22 Jan 2020.
Explore 6NPR in 3D Show helices and sheets RCSB PDB PDBe
6NPR contains 27 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 | 3-14 | 12 | 1 |
| β-strand | 18-28 | 11 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 51-54 | 4 | |
| 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 | 138-150 | 13 | |
| 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 | 199-208 | 10 | 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 | 241-249 | 9 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 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 |
| α-helix | 47 | 1 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 8 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 109-118 | 10 | 8 |
| β-strand | 121-126 | 6 | 8 |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 138-150 | 13 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 9 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 10 |
| β-strand | 199-208 | 10 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 213-219 | 7 | 11 |
| β-strand | 222-223 | 2 | 11 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-249 | 9 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-263 | 7 | 11 |
| β-strand | 270-272 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 5 |
| α-helix | 5-6 | 2 | |
| β-strand | 7-12 | 6 | 12 |
| β-strand | 22-31 | 10 | 12 |
| β-strand | 32 | 1 | 5 |
| β-strand | 37-42 | 6 | 13 |
| β-strand | 45-46 | 2 | 13 |
| β-strand | 51-52 | 2 | 12 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 12 |
| β-strand | 63-71 | 9 | 12 |
| β-strand | 79-84 | 6 | 13 |
| β-strand | 92-95 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class I histocompatibility antigen, D-D alpha chain | A, C | protein | 276 | Mus musculus | P01900 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Arg-gly-pro-gly-arg-ala-phe-val-thr-ile | P, R | protein | 10 | Human immunodeficiency virus 1 | P04578 (AlphaFold model) |
>6NPR_1 H-2 class I histocompatibility antigen, D-D alpha chain (chains A, C) SHSLRYFVTAVSRPGFGEPRYMEVGYVDNTEFVRFDSDAENPRYEPRARWIEQEGPEYWE RETRRAKGNEQSFRVDLRTALRCYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDGS DYIALNEDLKTWTAADMCAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLLR TDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGTF QKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRWGKE
>6NPR_2 Beta-2-microglobulin (chains B, D) MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>6NPR_3 ARG-GLY-PRO-GLY-ARG-ALA-PHE-VAL-THR-ILE (chains P, R) RGPGRAFVTI
Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection. McShan, A.C., Devlin, C.A., Overall, S.A. et al. Proc Natl Acad Sci U S A (2019) 116:25602-25613. DOI 10.1073/pnas.1915562116 · PubMed
Other PDB entries of the same protein (UniProt P01900 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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