1MHC: MHC class I antigen H2-M3

Model of MHC class I H2-M3 with nonapeptide from rat ND1 refined at 2.3 Å resolution. Determined by X-ray diffraction at 2.1 Å resolution. Released 29 Jan 1996.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Mus musculus, Rattus rattus
Chains
6
Atoms
6,668
Mol. weight
91.24 kDa
Ligands
NAG
Released
29 Jan 1996

Explore 1MHC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MHC contains 25 α-helices and 60 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.

Chain A: 10 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand3-12101
β-strand22-2871
β-strand31-3991
β-strand42-4761
α-helix50-523
α-helix58-8427
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-15013
α-helix153-1597
α-helix160-1645
α-helix165-17410
α-helix176-1794
β-strand18312
α-helix184-1852
β-strand186-19383
β-strand199-208103
β-strand20912
β-strand214-21964
β-strand222-22324
β-strand229-23023
α-helix231-2333
β-strand234-23523
β-strand241-24993
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chain B: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand35-4177
β-strand44-4527
β-strand50-5126
α-helix52-543
β-strand55-5626
β-strand62-7096
β-strand78-8477
β-strand91-9447
Chain D: 11 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
β-strand22-2878
β-strand31-3998
β-strand42-4768
α-helix50-545
α-helix57-8428
α-helix87-882
β-strand94-103108
β-strand109-118108
β-strand121-12668
β-strand133-13538
α-helix138-15013
α-helix152-1598
α-helix160-1645
α-helix165-17410
α-helix176-1794
β-strand18319
α-helix184-1852
β-strand186-193810
β-strand199-2081010
β-strand20919
β-strand214-219611
β-strand222-223211
β-strand229-230210
α-helix231-2333
β-strand234-235210
β-strand241-249910
α-helix253-2564
β-strand257-262611
β-strand270-272311
Chain E: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
α-helix4-52
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand35-41714
β-strand44-45214
α-helix461
β-strand50-51213
β-strand55-56213
β-strand62-70913
β-strand78-84714
β-strand91-94414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MHC class I antigen H2-M3A, Dprotein282Mus musculusQ31093 (AlphaFold model)
MHC class I antigen H2-M3B, Eprotein99Mus musculusP01887 (AlphaFold model)
Nonapeptide from rat NADH dehydrogenaseC, Fprotein9Rattus rattusP03889 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1MHC_1 MHC CLASS I ANTIGEN H2-M3 (chains A, D)
GSHSLRYFHTAVSRPGRGEPQYISVGYVDDVQFQRCDSIEEIPRMEPRAPWMEKERPEYW
KELKLKVKNIAQSARANLRTLLRYYNQSEGGSHILQWMVSCEVGPDMRLLGAHYQAAYDG
SDYITLNEDLSSWTAVDMVSQITKSRLESAGTAEYFRAYVEGECLELLHRFLRNGKEILQ
RADPPKAHVAHHPRPKGDVTLRCWALGFYPADITLTWQKDEEDLTQDMELVETRPSGDGT
FQKWAAVVVPSGEEQRYTCYVHHEGLTEPLALKWRSHHHHHH
Sequence of entity 2 (B, E), FASTA
>1MHC_2 MHC CLASS I ANTIGEN H2-M3 (chains B, E)
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
Sequence of entity 3 (C, F), FASTA
>1MHC_3 NONAPEPTIDE FROM RAT NADH DEHYDROGENASE (chains C, F)
MYFINILTL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O61

Primary citation

Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. Wang, C.R., Castano, A.R., Peterson, P.A. et al. Cell (1995) 82:655-664. DOI 10.1016/0092-8674(95)90037-3 · PubMed

Other PDB entries of the same protein (UniProt Q31093 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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