Crystal Structure of H-2D in complex with an insulin derived peptide. Determined by X-ray diffraction at 2.33 Å resolution. Released 26 Mar 2014.
Explore 3WS3 in 3D Show helices and sheets RCSB PDB PDBe
3WS3 contains 21 α-helices and 57 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 | 27-36 | 10 | 1 |
| α-helix | 44 | 1 | |
| β-strand | 45-52 | 8 | 1 |
| β-strand | 55-61 | 7 | 1 |
| β-strand | 70-71 | 2 | 1 |
| α-helix | 74-78 | 5 | |
| α-helix | 81-108 | 28 | |
| α-helix | 111-112 | 2 | |
| β-strand | 118-127 | 10 | 1 |
| β-strand | 133-142 | 10 | 1 |
| β-strand | 145-150 | 6 | 1 |
| β-strand | 157-159 | 3 | 1 |
| α-helix | 162-174 | 13 | |
| α-helix | 176-185 | 10 | |
| α-helix | 187-197 | 11 | |
| β-strand | 207 | 1 | 2 |
| α-helix | 208-209 | 2 | |
| β-strand | 210-217 | 8 | 3 |
| β-strand | 223-232 | 10 | 3 |
| β-strand | 233 | 1 | 2 |
| β-strand | 238-240 | 3 | 4 |
| β-strand | 253-254 | 2 | 3 |
| β-strand | 258-259 | 2 | 3 |
| β-strand | 265-273 | 9 | 3 |
| β-strand | 283-286 | 4 | 4 |
| β-strand | 294-296 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23 | 1 | 5 |
| β-strand | 26-31 | 6 | 6 |
| β-strand | 41-50 | 10 | 6 |
| β-strand | 51 | 1 | 5 |
| β-strand | 56-61 | 6 | 7 |
| β-strand | 64-65 | 2 | 7 |
| β-strand | 70-71 | 2 | 6 |
| α-helix | 72-74 | 3 | |
| β-strand | 75-76 | 2 | 6 |
| β-strand | 82-90 | 9 | 6 |
| β-strand | 98-103 | 6 | 7 |
| β-strand | 111-114 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-36 | 10 | 8 |
| β-strand | 45-52 | 8 | 8 |
| β-strand | 55-61 | 7 | 8 |
| β-strand | 70-71 | 2 | 8 |
| α-helix | 74-78 | 5 | |
| α-helix | 81-108 | 28 | |
| β-strand | 118-127 | 10 | 8 |
| β-strand | 133-142 | 10 | 8 |
| β-strand | 145-150 | 6 | 8 |
| β-strand | 157-159 | 3 | 8 |
| α-helix | 162-173 | 12 | |
| α-helix | 177-182 | 6 | |
| α-helix | 183-187 | 5 | |
| α-helix | 188-199 | 12 | |
| β-strand | 207 | 1 | 9 |
| α-helix | 208-209 | 2 | |
| β-strand | 210-217 | 8 | 10 |
| β-strand | 222-232 | 11 | 10 |
| β-strand | 233 | 1 | 9 |
| β-strand | 238-243 | 6 | 11 |
| β-strand | 246-248 | 3 | 11 |
| β-strand | 252-254 | 3 | 10 |
| β-strand | 258-259 | 2 | 10 |
| β-strand | 265-274 | 10 | 10 |
| α-helix | 278-280 | 3 | |
| β-strand | 282-286 | 5 | 11 |
| β-strand | 294-296 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| β-strand | 26-31 | 6 | 12 |
| α-helix | 34-35 | 2 | |
| β-strand | 41-50 | 10 | 12 |
| β-strand | 56-61 | 6 | 13 |
| β-strand | 64-65 | 2 | 13 |
| α-helix | 66 | 1 | |
| β-strand | 70-71 | 2 | 12 |
| α-helix | 72-74 | 3 | |
| β-strand | 75-76 | 2 | 12 |
| β-strand | 82-90 | 9 | 12 |
| β-strand | 98-103 | 6 | 13 |
| β-strand | 111-114 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class I histocompatibility antigen, D-B alpha chain | A, C | protein | 273 | Mus musculus | P01899 (AlphaFold model) |
| Beta-2-microglobulin | B, D | protein | 100 | Mus musculus | P01887 (AlphaFold model) |
| Insulin derived 9-mer peptide | E, F | protein | 9 | P01325 (AlphaFold model) |
>3WS3_1 H-2 class I histocompatibility antigen, D-B alpha chain (chains A, C) PHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWE RETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGR DYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLR TDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTF QKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRW
>3WS3_2 Beta-2-microglobulin (chains B, D) MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKD WSFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
>3WS3_3 Insulin derived 9-mer peptide (chains E, F) YQLENYCGL
Compensatory mechanisms allow undersized anchor-deficient class I MHC ligands to mediate pathogenic autoreactive T cell responses. Lamont, D., Mukherjee, G., Kumar, P.R. et al. J Immunol (2014) 193:2135-2146. DOI 10.4049/jimmunol.1400997 · PubMed
Other PDB entries of the same protein (UniProt P01899 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3WS3 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.