Complex between NK cell receptor Ly49A and its MHC class I ligand H-2Dd. Determined by X-ray diffraction at 2.3 Å resolution. Released 2 Jan 2000.
Explore 1QO3 in 3D Show helices and sheets RCSB PDB PDBe
1QO3 contains 19 α-helices and 45 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 | 138-150 | 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 |
| 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 | 229-230 | 2 | 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 | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 141-146 | 6 | 8 |
| β-strand | 149-158 | 10 | 8 |
| α-helix | 160-169 | 10 | |
| β-strand | 173-174 | 2 | 8 |
| α-helix | 180-189 | 10 | |
| β-strand | 195-202 | 8 | 8 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-210 | 4 | 8 |
| α-helix | 227-229 | 3 | |
| β-strand | 232-235 | 4 | 8 |
| β-strand | 240-243 | 4 | 8 |
| β-strand | 249-256 | 8 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 141-146 | 6 | 8 |
| β-strand | 149-158 | 10 | 8 |
| α-helix | 160-169 | 10 | |
| β-strand | 173-174 | 2 | 8 |
| α-helix | 180-189 | 10 | |
| β-strand | 195-202 | 8 | 8 |
| β-strand | 207-210 | 4 | 8 |
| α-helix | 222-224 | 3 | |
| α-helix | 227-229 | 3 | |
| β-strand | 232-235 | 4 | 8 |
| β-strand | 240-243 | 4 | 8 |
| β-strand | 249-256 | 8 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MHC class I H-2DD heavy chain | A | protein | 277 | MUS MUSCULUS | P01900 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 100 | MUS MUSCULUS | P01887 (AlphaFold model) |
| LY49A | C, D | protein | 137 | MUS MUSCULUS | P20937 (AlphaFold model) |
| HIV envelope glycoprotein 120 peptide | P | protein | 10 | HUMAN IMMUNODEFICIENCY VIRUS | P04582 |
>1QO3_1 MHC CLASS I H-2DD HEAVY CHAIN (chains A) MSHSLRYFVTAVSRPGFGEPRYMEVGYVDNTEFVRFDSDAENPRYEPRARWIEQEGPEYW ERETRRAKGNEQSFRVDLRTALRYYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDG CDYIALNEDLKTWTAADMAAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLL RTDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGT FQKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRWGKE
>1QO3_2 BETA-2-MICROGLOBULIN (chains B) MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKD WSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM
>1QO3_3 LY49A (chains C, D) STVLDSLQHTGRGDKVYWFCYGMKCYYFVMDRKTWSGCKQTCQSSSLSLLKIDDEDELKF LQLVVPSDSCWVGLSYDNKKKDWAWIDNRPSKLALNTRKYNIRDGGCMLLSKTRLDNGNC DQVFICICGKRLDKFPH
>1QO3_4 HIV ENVELOPE GLYCOPROTEIN 120 PEPTIDE (chains P) RGPGRAFVTI
Crystal Structure of a Lectin-Like Natural Killer Cell Receptor Bound to its Mhc Class I Ligand. Tormo, J., Natarajan, K., Margulies, D.H. et al. Nature (1999) 402:623. DOI 10.1038/45170 · 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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