MHC class I natural mutant H-2KBM1 heavy chain complexed with beta-2 microglobulin and vesicular stomatitis virus nucleoprotein. Determined by X-ray diffraction at 1.9 Å resolution. Released 28 Mar 2001.
Explore 1FZJ in 3D Show helices and sheets RCSB PDB PDBe
1FZJ contains 14 α-helices and 29 β-strands across 3 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 | 57-85 | 29 | |
| 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 | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| β-strand | 186-194 | 9 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 3 |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 258-262 | 5 | 4 |
| β-strand | 270-272 | 3 | 4 |
| 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 | |
| α-helix | 49 | 1 | |
| β-strand | 50-56 | 7 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H-2 class I histocompatibility antigen, K-B alpha chain | A | protein | 274 | Mus musculus | P01901 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Mus musculus | P01887 (AlphaFold model) |
| Nucleocapsid protein | P | protein | 8 | P11212 |
>1FZJ_1 H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN (chains A) GPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYW ERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDG CDYIALNEDLKTWTAADMAALITKHKWEQAGAAEYYRAYLEGTCVEWLRRYLKNGNATLL RTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGT FQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRW
>1FZJ_2 BETA-2-MICROGLOBULIN (chains B) IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW SFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
>1FZJ_3 NUCLEOCAPSID PROTEIN (chains P) RGYVYQGL
Water and common crystallization additives (MPD) are not listed.
The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity. Rudolph, M.G., Speir, J.A., Brunmark, A. et al. Immunity (2001) 14:231-242. DOI 10.1016/S1074-7613(01)00105-4 · 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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