Mhc Class I H-2Kb molecule complexed with pKB1 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Mar 2002.
Explore 1KJ3 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-150 | 13 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-179 | 15 | |
| β-strand | 183 | 1 | 2 |
| β-strand | 186-192 | 7 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 8 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 109-118 | 10 | 8 |
| β-strand | 121-126 | 6 | 8 |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-179 | 15 | |
| β-strand | 183 | 1 | 9 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 10 |
| β-strand | 198-208 | 11 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 214-219 | 6 | 11 |
| β-strand | 222-223 | 2 | 11 |
| β-strand | 228-230 | 3 | 10 |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-250 | 10 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 270-272 | 3 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| α-helix | 90 | 1 | |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 12 |
| β-strand | 6-11 | 6 | 13 |
| β-strand | 21-30 | 10 | 13 |
| β-strand | 31 | 1 | 12 |
| β-strand | 36-41 | 6 | 14 |
| β-strand | 44-45 | 2 | 14 |
| β-strand | 50-51 | 2 | 13 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 13 |
| β-strand | 62-70 | 9 | 13 |
| β-strand | 78-83 | 6 | 14 |
| β-strand | 91-94 | 4 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2KB MHC class I molecule alpha chain | H, I | protein | 279 | Mus musculus | P01901 (AlphaFold model) |
| Naturally processed octapeptide PKB1 | P, Q | protein | 8 | O08582 (AlphaFold model) | |
| Beta-2 microglobulin | L, M | protein | 99 | Mus musculus | P01887 (AlphaFold model) |
>1KJ3_1 H-2KB MHC CLASS I MOLECULE ALPHA CHAIN (chains H, I) MGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEY WERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYD GCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATL LRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDG TFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPP
>1KJ3_2 NATURALLY PROCESSED OCTAPEPTIDE PKB1 (chains P, Q) KVITFIDL
>1KJ3_3 BETA-2 MICROGLOBULIN (chains L, M) IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
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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