1KJ3: Mhc Class I H-2Kb molecule

Mhc Class I H-2Kb molecule complexed with pKB1 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Mar 2002.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Mus musculus
Chains
6
Atoms
6,694
Mol. weight
89.71 kDa
Released
27 Mar 2002

Explore 1KJ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KJ3 contains 25 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 H: 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-helix138-15013
α-helix152-1598
α-helix160-1645
α-helix165-17915
β-strand18312
β-strand186-19273
β-strand198-208113
β-strand20912
β-strand214-21964
β-strand222-22324
β-strand228-23033
α-helix231-2333
β-strand234-23523
β-strand241-250103
α-helix254-2563
β-strand257-26264
β-strand270-27234
Chain I: 9 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand3-12108
α-helix201
β-strand21-2888
β-strand31-3778
β-strand46-4728
α-helix50-545
α-helix57-8428
β-strand94-103108
β-strand109-118108
β-strand121-12668
β-strand133-13538
α-helix138-14912
α-helix152-1598
α-helix160-1645
α-helix165-17915
β-strand18319
α-helix184-1852
β-strand186-192710
β-strand198-2081110
β-strand20919
β-strand214-219611
β-strand222-223211
β-strand228-230310
β-strand234-235210
β-strand241-2501010
α-helix254-2563
β-strand257-262611
β-strand270-272311
Chain L: 4 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand315
α-helix4-52
β-strand6-1166
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
α-helix901
β-strand91-9447
Chain M: 1 helix, 11 β-strands
ElementResiduesLengthSheet
β-strand3112
β-strand6-11613
β-strand21-301013
β-strand31112
β-strand36-41614
β-strand44-45214
β-strand50-51213
α-helix52-543
β-strand55-56213
β-strand62-70913
β-strand78-83614
β-strand91-94414
Chains P and Q: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-54

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
H-2KB MHC class I molecule alpha chainH, Iprotein279Mus musculusP01901 (AlphaFold model)
Naturally processed octapeptide PKB1P, Qprotein8O08582 (AlphaFold model)
Beta-2 microglobulinL, Mprotein99Mus musculusP01887 (AlphaFold model)
Sequence of entity 1 (H, I), FASTA
>1KJ3_1 H-2KB MHC CLASS I MOLECULE ALPHA CHAIN (chains H, I)
MGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEY
WERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYD
GCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATL
LRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDG
TFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPP
Sequence of entity 2 (P, Q), FASTA
>1KJ3_2 NATURALLY PROCESSED OCTAPEPTIDE PKB1 (chains P, Q)
KVITFIDL
Sequence of entity 3 (L, M), FASTA
>1KJ3_3 BETA-2 MICROGLOBULIN (chains L, M)
IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW
SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM

Primary citation

A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Reiser, J.B., Gregoire, C., Darnault, C. et al. Immunity (2002) 16:345-354. DOI 10.1016/S1074-7613(02)00288-1 · 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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