5OQG: PDB entry 5OQG

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.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Mus musculus
Chains
2
Atoms
7,184
Mol. weight
96.13 kDa
Released
11 Apr 2018

Explore 5OQG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 12 helices, 30 β-strands

ElementResiduesLengthSheet
α-helix2-76
β-strand2611
α-helix27-282
β-strand29-3462
β-strand44-53102
β-strand5411
β-strand59-6463
β-strand67-6823
β-strand73-7422
α-helix75-773
β-strand78-7922
β-strand85-9392
β-strand101-10663
β-strand114-11743
β-strand145-154104
α-helix1621
β-strand163-17084
β-strand173-17974
β-strand188-18924
α-helix192-1943
α-helix199-22628
β-strand236-245104
β-strand251-260104
β-strand263-26864
β-strand275-27734
α-helix282-29211
α-helix294-3018
α-helix302-3065
α-helix307-31610
β-strand32515
α-helix326-3272
β-strand328-33586
β-strand340-350116
β-strand35115
β-strand356-36167
β-strand364-36527
β-strand371-37226
β-strand376-37726
β-strand383-392106
α-helix396-3983
β-strand399-40467
β-strand412-41437
Chain B: 13 helices, 30 β-strands
ElementResiduesLengthSheet
α-helix2-98
β-strand2618
α-helix27-282
β-strand29-3469
β-strand44-53109
β-strand5418
β-strand59-64610
β-strand67-68210
β-strand73-7429
α-helix75-773
β-strand78-7929
β-strand85-9399
β-strand101-106610
β-strand114-117410
β-strand145-1541011
α-helix1621
β-strand163-170811
β-strand173-179711
β-strand188-189211
α-helix192-1965
α-helix199-22628
β-strand236-2451011
β-strand251-2601011
β-strand263-268611
β-strand275-277311
α-helix280-29213
α-helix294-3007
α-helix301-3066
α-helix307-32115
β-strand325112
α-helix326-3272
β-strand328-335813
β-strand340-3501113
β-strand351112
β-strand356-361614
β-strand364-365214
β-strand371-372213
α-helix373-3753
β-strand376-377213
β-strand383-3921013
α-helix396-3983
β-strand399-404614
β-strand412-414314

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Beta-2-microglobulin,H-2 class I histocompatibility antigen, K-B alpha chainA, Bprotein431Mus musculusP01887 (AlphaFold model), P01901 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>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

Primary citation

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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