Crystal structure of a single chain trimer composed of the MHC I heavy chain H-2Kb W167A, beta-2microglobulin, and and ovalbumin-derived peptide. Determined by X-ray diffraction at 1.9 Å resolution. Released 11 Apr 2018.
Explore 5OQG in 3D Show helices and sheets RCSB PDB PDBe
5OQG contains 25 α-helices and 60 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 |
|---|---|---|---|
| α-helix | 2-7 | 6 | |
| β-strand | 26 | 1 | 1 |
| α-helix | 27-28 | 2 | |
| β-strand | 29-34 | 6 | 2 |
| β-strand | 44-53 | 10 | 2 |
| β-strand | 54 | 1 | 1 |
| β-strand | 59-64 | 6 | 3 |
| β-strand | 67-68 | 2 | 3 |
| β-strand | 73-74 | 2 | 2 |
| α-helix | 75-77 | 3 | |
| β-strand | 78-79 | 2 | 2 |
| β-strand | 85-93 | 9 | 2 |
| β-strand | 101-106 | 6 | 3 |
| β-strand | 114-117 | 4 | 3 |
| β-strand | 145-154 | 10 | 4 |
| α-helix | 162 | 1 | |
| β-strand | 163-170 | 8 | 4 |
| β-strand | 173-179 | 7 | 4 |
| β-strand | 188-189 | 2 | 4 |
| α-helix | 192-194 | 3 | |
| α-helix | 199-226 | 28 | |
| β-strand | 236-245 | 10 | 4 |
| β-strand | 251-260 | 10 | 4 |
| β-strand | 263-268 | 6 | 4 |
| β-strand | 275-277 | 3 | 4 |
| α-helix | 282-292 | 11 | |
| α-helix | 294-301 | 8 | |
| α-helix | 302-306 | 5 | |
| α-helix | 307-316 | 10 | |
| β-strand | 325 | 1 | 5 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-335 | 8 | 6 |
| β-strand | 340-350 | 11 | 6 |
| β-strand | 351 | 1 | 5 |
| β-strand | 356-361 | 6 | 7 |
| β-strand | 364-365 | 2 | 7 |
| β-strand | 371-372 | 2 | 6 |
| β-strand | 376-377 | 2 | 6 |
| β-strand | 383-392 | 10 | 6 |
| α-helix | 396-398 | 3 | |
| β-strand | 399-404 | 6 | 7 |
| β-strand | 412-414 | 3 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-9 | 8 | |
| β-strand | 26 | 1 | 8 |
| α-helix | 27-28 | 2 | |
| β-strand | 29-34 | 6 | 9 |
| β-strand | 44-53 | 10 | 9 |
| β-strand | 54 | 1 | 8 |
| β-strand | 59-64 | 6 | 10 |
| β-strand | 67-68 | 2 | 10 |
| β-strand | 73-74 | 2 | 9 |
| α-helix | 75-77 | 3 | |
| β-strand | 78-79 | 2 | 9 |
| β-strand | 85-93 | 9 | 9 |
| β-strand | 101-106 | 6 | 10 |
| β-strand | 114-117 | 4 | 10 |
| β-strand | 145-154 | 10 | 11 |
| α-helix | 162 | 1 | |
| β-strand | 163-170 | 8 | 11 |
| β-strand | 173-179 | 7 | 11 |
| β-strand | 188-189 | 2 | 11 |
| α-helix | 192-196 | 5 | |
| α-helix | 199-226 | 28 | |
| β-strand | 236-245 | 10 | 11 |
| β-strand | 251-260 | 10 | 11 |
| β-strand | 263-268 | 6 | 11 |
| β-strand | 275-277 | 3 | 11 |
| α-helix | 280-292 | 13 | |
| α-helix | 294-300 | 7 | |
| α-helix | 301-306 | 6 | |
| α-helix | 307-321 | 15 | |
| β-strand | 325 | 1 | 12 |
| α-helix | 326-327 | 2 | |
| β-strand | 328-335 | 8 | 13 |
| β-strand | 340-350 | 11 | 13 |
| β-strand | 351 | 1 | 12 |
| β-strand | 356-361 | 6 | 14 |
| β-strand | 364-365 | 2 | 14 |
| β-strand | 371-372 | 2 | 13 |
| α-helix | 373-375 | 3 | |
| β-strand | 376-377 | 2 | 13 |
| β-strand | 383-392 | 10 | 13 |
| α-helix | 396-398 | 3 | |
| β-strand | 399-404 | 6 | 14 |
| β-strand | 412-414 | 3 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin,H-2 class I histocompatibility antigen, K-B alpha chain | A, B | protein | 431 | Mus musculus | P01887 (AlphaFold model), P01901 (AlphaFold model) |
>5OQG_1 Beta-2-microglobulin,H-2 class I histocompatibility antigen, K-B alpha chain (chains A, B) SIINFEKLGCGASGGGGSGGGGSIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEI QMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDR DMGGGGSGGGGSGGGGSGGGGSGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDS DAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGCYNQSKGGSHTIQVI SGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRA YLEGTCVEALRRYLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQ LNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPP STVSNHHHHHH
The partial dissociation of MHC class I-bound peptides exposes their N terminus to trimming by endoplasmic reticulum aminopeptidase 1. Papakyriakou, A., Reeves, E., Beton, M. et al. J Biol Chem (2018) 293:7538-7548. DOI 10.1074/jbc.RA117.000313 · PubMed
Other PDB entries of the same protein (UniProt P01887 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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