Crystal structure of rat minor histocompatibility antigen complex RT1-aa/mtf-E. Determined by X-ray diffraction at 2.55 Å resolution. Released 28 Feb 2001.
Explore 1ED3 in 3D Show helices and sheets RCSB PDB PDBe
1ED3 contains 27 α-helices and 60 β-strands across 5 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 | 138-149 | 12 | |
| 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 | 213-219 | 7 | 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 | 257-263 | 7 | 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 |
| α-helix | 14-15 | 2 | |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| 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 | 3-12 | 10 | 8 |
| α-helix | 13-14 | 2 | |
| α-helix | 19-20 | 2 | |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 50-52 | 3 | |
| 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 | 138-149 | 12 | |
| 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 | 214-219 | 6 | 11 |
| β-strand | 223 | 1 | 11 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-230 | 3 | 10 |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-249 | 9 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 270-272 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 12 |
| β-strand | 6-11 | 6 | 13 |
| β-strand | 21-30 | 10 | 13 |
| β-strand | 31 | 1 | 12 |
| β-strand | 36-41 | 6 | 14 |
| β-strand | 44-45 | 2 | 14 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 13 |
| α-helix | 52-54 | 3 | |
| β-strand | 56 | 1 | 13 |
| β-strand | 62-70 | 9 | 13 |
| β-strand | 78-83 | 6 | 14 |
| β-strand | 91-94 | 4 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Class I major histocompatibility antigen RT1-aa | A, D | protein | 275 | Rattus norvegicus | P16391 (AlphaFold model) |
| Beta-2-microglobulin | B, E | protein | 99 | Rattus norvegicus | P07151 (AlphaFold model) |
| Peptide mtf-E (13N3E) | C, F | protein | 13 | P05504 (AlphaFold model) |
>1ED3_1 CLASS I MAJOR HISTOCOMPATIBILITY ANTIGEN RT1-AA (chains A, D) GSHSLRYFYTAVSRPGLGEPRFIAVGYVDDTEFVRFDSDAENPRMEPRARWMEREGPEYW EQQTRIAKEWEQIYRVDLRTLRGYYNQSEGGSHTIQEMYGCDVGSDGSLLRGYRQDAYDG RDYIALNEDLKTWTAADFAAQITRNKWERARYAERLRAYLEGTCVEWLSRYLELGKETLL RSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGT FQKWASVVVPLGKEQNYTCRVEHEGLPKPLSQRWE
>1ED3_2 BETA-2-MICROGLOBULIN (chains B, E) IQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDW SFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
>1ED3_3 PEPTIDE MTF-E (13N3E) (chains C, F) ILFPSSERLISNR
Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa. Speir, J.A., Stevens, J., Joly, E. et al. Immunity (2001) 14:81-92. DOI 10.1016/S1074-7613(01)00091-7 · 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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