1NAN: Mch class I H-2KB molecule

Mch class I H-2KB molecule complexed with PBM1 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 11 Mar 2003.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Mus musculus
Chains
6
Atoms
6,462
Mol. weight
89.51 kDa
Released
11 Mar 2003

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

Secondary structure: helices and β-sheets

1NAN contains 24 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 H: 10 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-helix138-15013
α-helix152-1587
α-helix159-1646
α-helix165-17410
β-strand18312
α-helix184-1852
β-strand186-19493
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
β-strand229-23023
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chain I: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
α-helix4-52
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
α-helix461
β-strand50-51213
β-strand55-56213
β-strand62-70913
β-strand78-83614
β-strand91-94414
Chain L: 11 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12105
α-helix201
β-strand21-2885
β-strand31-3775
β-strand46-4725
α-helix50-523
α-helix57-8428
β-strand94-103105
β-strand109-118105
β-strand121-12665
β-strand133-13535
α-helix140-14910
α-helix153-1586
α-helix159-1635
α-helix164-17512
β-strand18316
α-helix184-1852
β-strand186-19387
β-strand198-208117
β-strand20916
β-strand214-21968
β-strand222-22328
α-helix225-2273
β-strand229-23027
α-helix231-2333
β-strand234-23527
β-strand241-250107
α-helix254-2563
β-strand257-26268
β-strand270-27238
Chain P: 1 helix, 11 β-strands
ElementResiduesLengthSheet
β-strand319
β-strand6-11610
β-strand21-301010
β-strand3119
β-strand36-41611
β-strand44-45211
α-helix461
β-strand50-51210
β-strand55-56210
β-strand62-70910
β-strand78-83611
β-strand91-94411

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2 class I histocompatibility antigen, K-B alpha chainH, Lprotein278Mus musculusP01901 (AlphaFold model)
Beta-2-microglobulinI, Pprotein99Mus musculusP01887 (AlphaFold model)
pBM1 peptideM, Qprotein8Q8CDD8 (AlphaFold model)
Sequence of entity 1 (H, L), FASTA
>1NAN_1 H-2 class I histocompatibility antigen, K-B alpha chain (chains H, L)
GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYW
ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG
CDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLL
RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT
FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPP
Sequence of entity 2 (I, P), FASTA
>1NAN_2 Beta-2-microglobulin (chains I, P)
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
Sequence of entity 3 (M, Q), FASTA
>1NAN_3 pBM1 peptide (chains M, Q)
INFDFNTI

Primary citation

CDR3 loop flexibility contributes to the degeneracy of TCR recognition. Reiser, J.-B., Darnault, C., Gregoire, C. et al. Nat Immunol (2003) 4:241-247. DOI 10.1038/ni891 · 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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