1T0N: PDB entry 1T0N

Conformational switch in polymorphic H-2K molecules containing an HSV peptide. Determined by X-ray diffraction at 1.8 Å resolution. Released 23 Nov 2004.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Mus musculus
Chains
6
Atoms
7,000
Mol. weight
89.24 kDa
Released
23 Nov 2004

Explore 1T0N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1T0N contains 24 α-helices and 60 β-strands across 6 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-strand3-12101
α-helix201
β-strand21-2881
β-strand31-3771
β-strand46-4721
α-helix50-545
α-helix57-8428
β-strand94-103101
β-strand109-118101
β-strand121-12661
β-strand133-13531
α-helix138-14912
α-helix152-1587
α-helix159-1635
α-helix164-17916
β-strand18312
β-strand186-19273
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand221-22444
β-strand228-23033
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chains B and E: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
β-strand21-30106
β-strand3115
β-strand36-4167
β-strand44-4527
β-strand50-5126
α-helix52-543
β-strand55-5626
β-strand62-7096
β-strand78-8367
β-strand91-9447
Chain D: 9 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
α-helix201
β-strand21-2888
β-strand31-3778
β-strand46-4728
α-helix50-545
α-helix57-8529
β-strand94-103108
β-strand109-118108
β-strand121-12668
β-strand133-13538
α-helix138-15013
α-helix152-1598
α-helix160-1645
α-helix165-17915
β-strand18319
β-strand186-192710
β-strand198-2081110
β-strand20919
β-strand214-219611
β-strand223111
β-strand229-230210
α-helix231-2333
β-strand234-235210
β-strand241-2501010
α-helix254-2563
β-strand257-262611
β-strand270-272311
Chains P and Q: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-76

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class I histocompatibility antigen, K-B alpha chainA, Dprotein278Mus musculusP01901 (AlphaFold model)
Beta-2-microglobulinB, Eprotein99Mus musculusP01887 (AlphaFold model)
Glycoprotein BP, Qprotein8P06436
Sequence of entity 1 (A, D), FASTA
>1T0N_1 H-2 class I histocompatibility antigen, K-B alpha chain (chains A, D)
GPHSLRYFVTAVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRYEPRARWMEQEGPEYW
ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG
CDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLL
RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT
FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPP
Sequence of entity 2 (B, E), FASTA
>1T0N_2 Beta-2-microglobulin (chains B, E)
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
Sequence of entity 3 (P, Q), FASTA
>1T0N_3 Glycoprotein B (chains P, Q)
SSIEFARL

Primary citation

The structure of H-2K(b) and K(bm8) complexed to a herpes simplex virus determinant: evidence for a conformational switch that governs T cell repertoire selection and viral resistance. Webb, A.I., Borg, N.A., Dunstone, M.A. et al. J Immunol (2004) 173:402-409. DOI 10.4049/jimmunol.173.1.402 · PubMed

Other PDB entries of the same protein (UniProt P01901 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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