7JI2: H2-Kb
Crystal Structure of H2-Kb in complex with a OVA mutant peptide. Determined by X-ray diffraction at 1.95 Å resolution. Released 23 Dec 2020.
- Method
- X-ray diffraction
- Resolution
- 1.95 Å
- Organisms
- Mus musculus bactrianus, synthetic construct
- Chains
- 6
- Atoms
- 6,866
- Mol. weight
- 91.16 kDa
- Released
- 23 Dec 2020
Explore 7JI2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7JI2 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 A: 10 helices, 19 β-strands
| 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 | 50-52 | 3 | |
| 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 | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-179 | 15 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 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 | 229-230 | 2 | 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 |
Chain B: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 5 |
| 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 |
| 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 |
| β-strand | 91-94 | 4 | 7 |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
Chain D: 9 helices, 19 β-strands
| 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 | 50-52 | 3 | |
| α-helix | 57-85 | 29 | |
| 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 | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-179 | 16 | |
| β-strand | 183 | 1 | 9 |
| β-strand | 186-194 | 9 | 10 |
| β-strand | 198-208 | 11 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 214-219 | 6 | 11 |
| β-strand | 222-223 | 2 | 11 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 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 |
Chain E: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 12 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 13 |
| α-helix | 14-15 | 2 | |
| 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 |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-7 | 6 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| H-2 class I histocompatibility antigen, K-B alpha chain | A, D | protein | 281 | Mus musculus bactrianus | P01901 (AlphaFold model) |
| Beta-2-microglobulin | B, E | protein | 100 | Mus musculus bactrianus | P01887 (AlphaFold model) |
| OVA mutant peptide | C, F | protein | 8 | synthetic construct | |
Sequence of entity 1 (A, D), FASTA
>7JI2_1 H-2 class I histocompatibility antigen, K-B alpha chain (chains A, D)
MGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEY
WERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYD
GCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATL
LRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDG
TFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPST
Sequence of entity 2 (B, E), FASTA
>7JI2_2 Beta-2-microglobulin (chains B, E)
MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKD
WSFYILAHTEFTPTETDTYACRVKHDSMAEPKTVYWDRDM
Sequence of entity 3 (C, F), FASTA
>7JI2_3 OVA mutant peptide (chains C, F)
SIIQFEHL
Primary citation
Pre-T cell receptors topologically sample self-ligands during thymocyte beta-selection. Li, X., Mizsei, R., Tan, K. et al. Science (2021) 371:181-185. DOI 10.1126/science.abe0918 · PubMed
Other PDB entries of the same protein (UniProt P01901 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1LK2 1.35 Å, 1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide
- 1G7P 1.5 Å, Crystal structure of MHC class I H-2KB heavy chain complexed with beta-2 microglobulin…
- 1KPU 1.5 Å, High resolution crystal structure of the MHC class I complex H-2Kb/VSV8
- 1G7Q 1.6 Å, Crystal structure of MHC class I H-2KB heavy chain complexed with beta-2 microglobulin…
- 3TID 1.65 Å, Crystal structure of the LCMV derived peptide GP34 in complex with the murine mhc class…
- 1FZK 1.7 Å, MHC class I natural mutant H-2KBM1 heavy chain complexed with beta-2 microglobulin and…
- 1KPV 1.71 Å, High resolution crystal structure of the MHC class I complex H-2Kb/SEV9
- 1LEG 1.75 Å, Crystal Structure of H-2Kb bound to the dEV8 peptide
- 6GB6 1.78 Å, Structure of H-2Kb with dipeptide GL
- 1FZM 1.8 Å, MHC class I natural mutant H-2KBM8 heavy chain complexed with beta-2 microglobulin and…
- 1FZO 1.8 Å, MHC class I natural mutant H-2KBM8 heavy chain complexed with beta-2 microglobulin and…
- 1T0N 1.8 Å, Conformational switch in polymorphic H-2K molecules containing an HSV peptide
Browse structure collections
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