9GV6: TCR
Structure of TCR in complex with peptide-HLA. Determined by X-ray diffraction at 2.77 Å resolution. Released 23 Apr 2025.
- Method
- X-ray diffraction
- Resolution
- 2.77 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 13,165
- Mol. weight
- 189.53 kDa
- Released
- 23 Apr 2025
Explore 9GV6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9GV6 contains 42 α-helices and 144 β-strands across 8 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 | 3-14 | 12 | 1 |
| β-strand | 18-28 | 11 | 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 | 139-149 | 11 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 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 | 222-224 | 3 | 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 |
Chain B: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-8 | 3 | 6 |
| β-strand | 11 | 1 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 45 | 1 | 7 |
| β-strand | 50-51 | 2 | 6 |
| 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 D: 3 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6 | 1 | 8 |
| β-strand | 10-14 | 5 | 9 |
| β-strand | 19-24 | 6 | 8 |
| β-strand | 33-39 | 7 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 56-57 | 2 | 8 |
| β-strand | 62-64 | 3 | 8 |
| β-strand | 71-76 | 6 | 8 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 9 |
| β-strand | 94 | 1 | 10 |
| β-strand | 104-109 | 6 | 9 |
| β-strand | 118-123 | 6 | 11 |
| β-strand | 124 | 1 | 12 |
| β-strand | 131-138 | 8 | 11 |
| β-strand | 153-154 | 2 | 11 |
| α-helix | 155-157 | 3 | |
| β-strand | 158-161 | 4 | 11 |
| α-helix | 163-165 | 3 | |
| β-strand | 168-175 | 8 | 11 |
Chain E: 7 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 13 |
| β-strand | 11-15 | 5 | 14 |
| β-strand | 20-25 | 6 | 13 |
| β-strand | 32-38 | 7 | 14 |
| β-strand | 45-51 | 7 | 14 |
| β-strand | 54-57 | 4 | 14 |
| β-strand | 66-67 | 2 | 13 |
| β-strand | 76-80 | 5 | 13 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-96 | 8 | 14 |
| β-strand | 103 | 1 | 10 |
| α-helix | 104-106 | 3 | |
| β-strand | 107-108 | 2 | 14 |
| β-strand | 112-117 | 6 | 14 |
| α-helix | 120-122 | 3 | |
| β-strand | 124 | 1 | 15 |
| β-strand | 127-131 | 5 | 12 |
| α-helix | 132-134 | 3 | |
| α-helix | 135-141 | 7 | |
| β-strand | 143-153 | 11 | 12 |
| β-strand | 154 | 1 | 15 |
| β-strand | 158-164 | 7 | 16 |
| β-strand | 167-169 | 3 | 16 |
| β-strand | 173-175 | 3 | 12 |
| β-strand | 180-181 | 2 | 12 |
| β-strand | 191-200 | 10 | 12 |
| α-helix | 201-205 | 5 | |
| β-strand | 210-217 | 8 | 16 |
| β-strand | 220 | 1 | 17 |
| α-helix | 231-232 | 2 | |
| β-strand | 234 | 1 | 17 |
| β-strand | 236-243 | 8 | 16 |
Chain G: 10 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 18 |
| β-strand | 21-28 | 8 | 18 |
| β-strand | 31-37 | 7 | 18 |
| β-strand | 46-47 | 2 | 18 |
| α-helix | 50-54 | 5 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 18 |
| β-strand | 109-118 | 10 | 18 |
| β-strand | 121-126 | 6 | 18 |
| β-strand | 133-135 | 3 | 18 |
| α-helix | 139-149 | 11 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 19 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 20 |
| β-strand | 198-208 | 11 | 20 |
| β-strand | 209 | 1 | 19 |
| β-strand | 214-219 | 6 | 21 |
| β-strand | 222-224 | 3 | 21 |
| β-strand | 228-230 | 3 | 20 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 20 |
| β-strand | 241-250 | 10 | 20 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 21 |
| β-strand | 270-272 | 3 | 21 |
Chain H: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 22 |
| β-strand | 6-11 | 6 | 23 |
| β-strand | 21-30 | 10 | 23 |
| β-strand | 31 | 1 | 22 |
| β-strand | 36-41 | 6 | 24 |
| β-strand | 45 | 1 | 24 |
| β-strand | 50-51 | 2 | 23 |
| β-strand | 55-56 | 2 | 23 |
| β-strand | 62-70 | 9 | 23 |
| β-strand | 78-83 | 6 | 24 |
| α-helix | 90 | 1 | |
| β-strand | 91-92 | 2 | 24 |
Chain J: 3 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6 | 1 | 25 |
| β-strand | 10-14 | 5 | 26 |
| β-strand | 19-24 | 6 | 25 |
| β-strand | 33-39 | 7 | 26 |
| β-strand | 46-51 | 6 | 26 |
| β-strand | 56-57 | 2 | 25 |
| β-strand | 62-64 | 3 | 25 |
| β-strand | 71-76 | 6 | 25 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-92 | 7 | 26 |
| α-helix | 96-98 | 3 | |
| β-strand | 104-109 | 6 | 26 |
| β-strand | 118-123 | 6 | 27 |
| β-strand | 131-136 | 6 | 27 |
| α-helix | 142-147 | 6 | |
| β-strand | 153-154 | 2 | 27 |
| β-strand | 159-160 | 2 | 28 |
| β-strand | 171-175 | 5 | 27 |
Chain K: 7 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 29 |
| β-strand | 11-15 | 5 | 30 |
| β-strand | 17 | 1 | 31 |
| β-strand | 20-25 | 6 | 29 |
| β-strand | 32-39 | 8 | 30 |
| β-strand | 45-51 | 7 | 30 |
| β-strand | 54-57 | 4 | 30 |
| β-strand | 66-67 | 2 | 29 |
| β-strand | 76-80 | 5 | 29 |
| β-strand | 83 | 1 | 31 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-96 | 8 | 30 |
| α-helix | 104-106 | 3 | |
| β-strand | 107-108 | 2 | 30 |
| β-strand | 112-117 | 6 | 30 |
| α-helix | 120-122 | 3 | |
| β-strand | 124 | 1 | 32 |
| α-helix | 125-126 | 2 | |
| β-strand | 127-131 | 5 | 28 |
| α-helix | 132-134 | 3 | |
| α-helix | 135-141 | 7 | |
| β-strand | 143-153 | 11 | 28 |
| β-strand | 154 | 1 | 32 |
| β-strand | 158-164 | 7 | 8 |
| β-strand | 167-169 | 3 | 8 |
| β-strand | 173-175 | 3 | 28 |
| β-strand | 180-181 | 2 | 28 |
| β-strand | 191-200 | 10 | 28 |
| α-helix | 201-205 | 5 | |
| β-strand | 210-217 | 8 | 8 |
| β-strand | 220 | 1 | 33 |
| β-strand | 234 | 1 | 33 |
| β-strand | 236-243 | 8 | 8 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MHC class I antigen | A, G | protein | 276 | Homo sapiens | A0A5B8RNS7 (AlphaFold model) |
| Beta-2-microglobulin | B, H | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Peptide | C, I | protein | 9 | Homo sapiens | |
| TCR alpha | D, J | protein | 196 | Homo sapiens | |
| TCR Beta | E, K | protein | 247 | Homo sapiens | |
Sequence of entity 1 (A, G), FASTA
>9GV6_1 MHC class I antigen (chains A, G)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, H), FASTA
>9GV6_2 Beta-2-microglobulin (chains B, H)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, I), FASTA
>9GV6_3 Peptide (chains C, I)
SLSNRLYYL
Sequence of entity 4 (D, J), FASTA
>9GV6_4 TCR alpha (chains D, J)
MLAKTTQPISMDSYEGQEVNITCSHNHIAANDFITWYQQFPSQGPRFFIQGYKTNVSNEV
ASLFIPADRKSSTLSLPRVSLSDTAVYYCLAWGGTDMLIFGTGTRLQVFPNIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFNNSIIPEDT
Sequence of entity 5 (E, K), FASTA
>9GV6_5 TCR Beta (chains E, K)
MEAGVAQSPRYKIIEKRQSVAFWCNPISGHGTLYWYQQILGQGPKLLIQFHNNGVVDDSQ
LPKDRFSAERLKGVDSTLKIQPAKLEDSAVYLCASSLDWVGDGERQYFGPGTRLLVLEDL
KNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPL
KEQPALNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSA
EAWGRAD
Primary citation
Determining T-cell receptor binding orientation and Peptide-HLA interactions using cross-linking mass spectrometry. Powell, T., Karuppiah, V., Shaikh, S.A. et al. J Biol Chem (2025) 301:108445-108445. DOI 10.1016/j.jbc.2025.108445 · PubMed
Other PDB entries of the same protein (UniProt A0A5B8RNS7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9GV7 1.86 Å, Structure of reverse docking TCR in complex with peptide-HLA
- 6TMO 2.1 Å, Structure determination of an enhanced affinity TCR, a24b17, in complex with HLA-A*02:01…
- 9DL1 2.3 Å, Crystal Structure of HLA-A*02:01/NY-ESO-1 (SLLMWITQV) and a target specific TRACeR-I
- 9SOK 2.5 Å, Structure of three-domain single chain TCR-581 in complex with Peptide-HLA
- 9SOL 2.93 Å, Structure of TCR-581 in complex with Peptide-HLA
Browse structure collections
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