TCR55 in complex with Pep20/HLA-B35. Determined by X-ray diffraction at 1.75 Å resolution. Released 25 Jul 2018.
Explore 6BJ8 in 3D Show helices and sheets RCSB PDB PDBe
6BJ8 contains 33 α-helices and 73 β-strands across 5 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 | 4-12 | 9 | 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 | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| 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 |
| α-helix | 225-227 | 3 | |
| 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 |
| 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 |
| β-strand | 91-94 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 8 |
| β-strand | 10-14 | 5 | 9 |
| β-strand | 19-21 | 3 | 8 |
| β-strand | 23-25 | 3 | 8 |
| β-strand | 32-39 | 8 | 9 |
| β-strand | 45-52 | 8 | 9 |
| α-helix | 56-58 | 3 | |
| β-strand | 59-60 | 2 | 8 |
| β-strand | 63-68 | 6 | 8 |
| β-strand | 73-78 | 6 | 8 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-95 | 9 | 9 |
| β-strand | 102-103 | 2 | 9 |
| β-strand | 107-112 | 6 | 9 |
| α-helix | 113 | 1 | |
| β-strand | 121-124 | 4 | 10 |
| α-helix | 125 | 1 | |
| β-strand | 126 | 1 | 11 |
| α-helix | 127-128 | 2 | |
| β-strand | 134-139 | 6 | 10 |
| β-strand | 155-157 | 3 | 10 |
| α-helix | 158-160 | 3 | |
| β-strand | 161-165 | 5 | 10 |
| α-helix | 166-168 | 3 | |
| β-strand | 170-179 | 10 | 10 |
| α-helix | 186-189 | 4 | |
| β-strand | 200 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 31-37 | 7 | 13 |
| β-strand | 43-49 | 7 | 13 |
| α-helix | 57-59 | 3 | |
| α-helix | 61 | 1 | |
| β-strand | 64-68 | 5 | 12 |
| β-strand | 73-78 | 6 | 12 |
| α-helix | 83-85 | 3 | |
| β-strand | 87-94 | 8 | 13 |
| α-helix | 102-103 | 2 | |
| β-strand | 104-105 | 2 | 13 |
| β-strand | 109-114 | 6 | 13 |
| α-helix | 117-119 | 3 | |
| β-strand | 121 | 1 | 14 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-128 | 5 | 15 |
| β-strand | 129 | 1 | 11 |
| α-helix | 130-131 | 2 | |
| α-helix | 132-138 | 7 | |
| β-strand | 140-150 | 11 | 15 |
| β-strand | 151 | 1 | 14 |
| β-strand | 155-161 | 7 | 16 |
| β-strand | 164-166 | 3 | 16 |
| β-strand | 170-172 | 3 | 15 |
| β-strand | 177-178 | 2 | 15 |
| β-strand | 188-197 | 10 | 15 |
| α-helix | 198-201 | 4 | |
| β-strand | 207-214 | 8 | 16 |
| β-strand | 217 | 1 | 17 |
| α-helix | 228-229 | 2 | |
| β-strand | 231 | 1 | 17 |
| β-strand | 233-240 | 8 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| HLA class I histocompatibility antigen, B-35 alpha chain | A | protein | 276 | Homo sapiens | P01889 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| TCR 55 alpha chain | D | protein | 204 | Homo sapiens | Q6IRV4 (AlphaFold model) |
| TCR 55 beta chain | H | protein | 242 | Homo sapiens | K7N5M4 (AlphaFold model) |
| Val-pro-leu-thr-glu-asp-ala-glu-leu | C | protein | 9 | synthetic construct |
>6BJ8_1 HLA class I histocompatibility antigen, B-35 alpha chain (chains A) GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW DRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQ RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
>6BJ8_2 Beta-2-microglobulin (chains B) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>6BJ8_3 TCR 55 alpha chain (chains D) MQKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKS GRYSVNFKKAAKSVALTISALQLEDSAKYFCALGEGGAQKLVFGQGTRLTINPNIQNPDP AVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSN KSDFACANAFNNSIIPEDTFFPSP
>6BJ8_4 TCR 55 beta chain (chains H) GVTQTPKFQVLKTGQSMTLQCAQDMNHNSMYWYRQDPGMGLRLIYYSASEGTTDKGEVPN GYNVSRLNKREFSLRLESAAPSQTSVYFCASRTRGGTLIEQYFGPGTRLTVTEDLKNVFP PEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPA LNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR AD
>6BJ8_5 VAL-PRO-LEU-THR-GLU-ASP-ALA-GLU-LEU (chains C) VPLTEDAEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 4 |
Water and common crystallization additives (GOL) are not listed.
Isolation of a Structural Mechanism for Uncoupling T Cell Receptor Signaling from Peptide-MHC Binding. Sibener, L.V., Fernandes, R.A., Kolawole, E.M. et al. Cell (2018) 174:672-687.e27. DOI 10.1016/j.cell.2018.06.017 · PubMed
Other PDB entries of the same protein (UniProt P01889 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6BJ8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.