1ED3: Class I major histocompatibility antigen RT1-aa

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.

Method
X-ray diffraction
Resolution
2.55 Å
Organism
Rattus norvegicus
Chains
6
Atoms
6,519
Mol. weight
90.46 kDa
Released
28 Feb 2001

Explore 1ED3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 9 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand2-12111
α-helix201
β-strand21-2881
β-strand31-3771
β-strand46-4721
α-helix50-523
α-helix57-8428
β-strand94-104111
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-16110
α-helix163-17412
α-helix176-1794
β-strand18312
α-helix184-1852
β-strand186-19383
β-strand199-208103
β-strand20912
β-strand213-21974
β-strand222-22324
β-strand229-23023
β-strand234-23523
β-strand241-24993
α-helix254-2563
β-strand257-26374
β-strand270-27234
Chain B: 4 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
α-helix14-152
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
α-helix461
β-strand50-5126
α-helix52-543
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain D: 11 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
α-helix13-142
α-helix19-202
β-strand21-2888
β-strand31-3778
β-strand46-4728
α-helix50-523
α-helix57-8428
β-strand94-103108
β-strand109-118108
β-strand121-12668
β-strand133-13538
α-helix138-14912
α-helix152-16110
α-helix163-17412
α-helix176-1794
β-strand18319
α-helix184-1852
β-strand186-193810
β-strand199-2081010
β-strand20919
β-strand214-219611
β-strand223111
α-helix225-2273
β-strand228-230310
β-strand234-235210
β-strand241-249910
α-helix254-2563
β-strand257-262611
β-strand270-272311
Chain E: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
α-helix461
β-strand50-51213
α-helix52-543
β-strand56113
β-strand62-70913
β-strand78-83614
β-strand91-94414
Chain F: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-54

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Class I major histocompatibility antigen RT1-aaA, Dprotein275Rattus norvegicusP16391 (AlphaFold model)
Beta-2-microglobulinB, Eprotein99Rattus norvegicusP07151 (AlphaFold model)
Peptide mtf-E (13N3E)C, Fprotein13P05504 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1ED3_1 CLASS I MAJOR HISTOCOMPATIBILITY ANTIGEN RT1-AA (chains A, D)
GSHSLRYFYTAVSRPGLGEPRFIAVGYVDDTEFVRFDSDAENPRMEPRARWMEREGPEYW
EQQTRIAKEWEQIYRVDLRTLRGYYNQSEGGSHTIQEMYGCDVGSDGSLLRGYRQDAYDG
RDYIALNEDLKTWTAADFAAQITRNKWERARYAERLRAYLEGTCVEWLSRYLELGKETLL
RSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGT
FQKWASVVVPLGKEQNYTCRVEHEGLPKPLSQRWE
Sequence of entity 2 (B, E), FASTA
>1ED3_2 BETA-2-MICROGLOBULIN (chains B, E)
IQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDW
SFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM
Sequence of entity 3 (C, F), FASTA
>1ED3_3 PEPTIDE MTF-E (13N3E) (chains C, F)
ILFPSSERLISNR

Primary citation

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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