TAP-A-associated rat MHC class I molecule. Determined by X-ray diffraction at 2.35 Å resolution. Released 18 Dec 2002.
Explore 1KJM in 3D Show helices and sheets RCSB PDB PDBe
1KJM contains 10 α-helices and 31 β-strands across 2 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 | 2-12 | 11 | 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 | 94-104 | 11 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 139-149 | 11 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| 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 |
| 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 | 1 | 6 |
| β-strand | 9-11 | 3 | 7 |
| β-strand | 21-30 | 10 | 7 |
| β-strand | 31 | 1 | 5 |
| β-strand | 35-41 | 7 | 8 |
| β-strand | 44-45 | 2 | 8 |
| β-strand | 50-51 | 2 | 7 |
| β-strand | 55-56 | 2 | 7 |
| β-strand | 62-70 | 9 | 7 |
| β-strand | 78-84 | 7 | 8 |
| β-strand | 92-94 | 3 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RT1 class I histocompatibility antigen, AA alpha chain, heavy chain | A | protein | 285 | Rattus norvegicus | P16391 (AlphaFold model) |
| beta-2-Microglobulin | B | protein | 100 | Rattus norvegicus | P07151 (AlphaFold model) |
| B6 Peptide | P | protein | 9 |
>1KJM_1 RT1 class I histocompatibility antigen, AA alpha chain, heavy chain (chains A) GSHSLRYFYTAVSRPGLGEPRFIAVGYVDDTEFVRFDSDAENPRMEPRARWMEREGPEYW EQQTRIAKEWEQIYRVDLRTLRGYYNQSEGGSHTIQEMYGCDVGSDGSLLRGYRQDAYDG RDYIALNEDLKTWTAADFAAQITRNKWERARYAERLRAYLEGTCVEWLSRYLELGKETLL RSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGT FQKWASVVVPLGKEQNYTCRVEHEGLPKPLSQRWEPLLEHHHHHH
>1KJM_2 beta-2-Microglobulin (chains B) MIQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKD WSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
>1KJM_3 B6 Peptide (chains P) AQFSASASR
Crystal structures of two rat MHC class Ia (RT1-A) molecules that are associated differentially with peptide transporter alleles TAP-A and TAP-B. Rudolph, M.G., Stevens, J., Speir, J.A. et al. J Mol Biol (2002) 324:975-990. DOI 10.1016/S0022-2836(02)01095-1 · PubMed
Other PDB entries of the same protein (UniProt P16391 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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