Cryo-EM structure of the gdTCR-ECD. Determined by electron microscopy at 2.9 Å resolution. Released 7 May 2025.
Explore 8ZD4 in 3D Show helices and sheets RCSB PDB PDBe
8ZD4 contains 22 α-helices and 89 β-strands across 4 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 | 23-25 | 3 | 1 |
| β-strand | 31-34 | 4 | 2 |
| β-strand | 41-46 | 6 | 1 |
| β-strand | 53-60 | 8 | 3 |
| β-strand | 64-70 | 7 | 3 |
| β-strand | 78-80 | 3 | 1 |
| β-strand | 83-88 | 6 | 1 |
| β-strand | 93-98 | 6 | 1 |
| α-helix | 103-105 | 3 | |
| β-strand | 108 | 1 | 3 |
| β-strand | 111-115 | 5 | 3 |
| β-strand | 123-126 | 4 | 3 |
| β-strand | 132-135 | 4 | 2 |
| β-strand | 142 | 1 | 4 |
| β-strand | 146-150 | 5 | 5 |
| β-strand | 154 | 1 | 6 |
| β-strand | 155-162 | 8 | 5 |
| β-strand | 163 | 1 | 4 |
| β-strand | 168-172 | 5 | 7 |
| β-strand | 176-179 | 4 | 6 |
| α-helix | 185 | 1 | |
| β-strand | 186 | 1 | 5 |
| α-helix | 187 | 1 | |
| β-strand | 192-196 | 5 | 5 |
| β-strand | 198-200 | 3 | 6 |
| β-strand | 207-212 | 6 | 7 |
| β-strand | 215-217 | 3 | 7 |
| α-helix | 220-222 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-31 | 5 | 8 |
| β-strand | 37-41 | 5 | 9 |
| β-strand | 50-53 | 4 | 10 |
| β-strand | 56 | 1 | 8 |
| β-strand | 62 | 1 | 8 |
| β-strand | 66-69 | 4 | 10 |
| β-strand | 74-77 | 4 | 10 |
| α-helix | 78 | 1 | |
| α-helix | 81-82 | 2 | |
| β-strand | 86-89 | 4 | 9 |
| β-strand | 96-100 | 5 | 9 |
| α-helix | 105-107 | 3 | |
| β-strand | 109-110 | 2 | 8 |
| β-strand | 113-117 | 5 | 10 |
| β-strand | 127-130 | 4 | 10 |
| β-strand | 134-138 | 5 | 8 |
| β-strand | 150-154 | 5 | 11 |
| α-helix | 155-157 | 3 | |
| α-helix | 160-164 | 5 | |
| β-strand | 167-176 | 10 | 11 |
| β-strand | 183-186 | 4 | 12 |
| α-helix | 193-195 | 3 | |
| β-strand | 197-198 | 2 | 11 |
| β-strand | 202-203 | 2 | 11 |
| β-strand | 208-216 | 9 | 11 |
| α-helix | 218-220 | 3 | |
| β-strand | 225-229 | 5 | 12 |
| α-helix | 235-237 | 3 | |
| β-strand | 240-244 | 5 | 12 |
| α-helix | 245-247 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 23-25 | 3 | 13 |
| β-strand | 30-34 | 5 | 14 |
| β-strand | 39-46 | 8 | 13 |
| β-strand | 53-59 | 7 | 14 |
| β-strand | 65 | 1 | 14 |
| β-strand | 69-70 | 2 | 14 |
| β-strand | 79-80 | 2 | 13 |
| β-strand | 83-88 | 6 | 13 |
| β-strand | 93-98 | 6 | 13 |
| β-strand | 108-115 | 8 | 14 |
| β-strand | 123-126 | 4 | 14 |
| β-strand | 130-135 | 6 | 14 |
| α-helix | 136-138 | 3 | |
| β-strand | 142 | 1 | 15 |
| β-strand | 146-150 | 5 | 16 |
| β-strand | 154 | 1 | 17 |
| β-strand | 155-162 | 8 | 16 |
| β-strand | 163 | 1 | 15 |
| β-strand | 168-172 | 5 | 18 |
| β-strand | 178-179 | 2 | 17 |
| β-strand | 185 | 1 | 19 |
| β-strand | 192 | 1 | 16 |
| β-strand | 193 | 1 | 19 |
| β-strand | 194-196 | 3 | 16 |
| β-strand | 198-199 | 2 | 17 |
| α-helix | 203-205 | 3 | |
| β-strand | 207-212 | 6 | 18 |
| β-strand | 215-217 | 3 | 18 |
| α-helix | 220-222 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 27-32 | 6 | 20 |
| β-strand | 37-40 | 4 | 21 |
| β-strand | 50-56 | 7 | 20 |
| β-strand | 62-69 | 8 | 20 |
| β-strand | 74-76 | 3 | 20 |
| α-helix | 81-82 | 2 | |
| β-strand | 86-92 | 7 | 21 |
| β-strand | 95-100 | 6 | 21 |
| α-helix | 105-107 | 3 | |
| β-strand | 109-117 | 9 | 20 |
| β-strand | 127-130 | 4 | 20 |
| β-strand | 134-139 | 6 | 20 |
| β-strand | 150-154 | 5 | 22 |
| α-helix | 155-157 | 3 | |
| α-helix | 158-164 | 7 | |
| β-strand | 166-174 | 9 | 22 |
| β-strand | 182-186 | 5 | 23 |
| β-strand | 197-198 | 2 | 22 |
| β-strand | 202-203 | 2 | 22 |
| β-strand | 208-217 | 10 | 22 |
| α-helix | 218-220 | 3 | |
| β-strand | 225-230 | 6 | 23 |
| α-helix | 235-237 | 3 | |
| β-strand | 240-244 | 5 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TRA@ protein | A, D | protein | 202 | Homo sapiens | Q6PJ56 (AlphaFold model) |
| gamma chain | B, G | protein | 224 | Homo sapiens |
>8ZD4_1 TRA@ protein (chains A, D) QKVTQAQSSVSMPVRKAVTLNCLYETSWWSYYIFWYKQLPSKEMIFLIRQGSDEQNAKSG RYSVNFKKAAKSVALTISALQLEDSAKYFCALGDPGGLNTDKLIFGKGTRVTVEPRSQPH TKPSVFVMKNGTNVACLVKEFYPKDIRINLVSSKKITEFDPAIVISPSGKYNAVKLGKYE DSNSVTCSVQHDNKTVHSTDFE
>8ZD4_2 gamma chain (chains B, G) GTKSVTRPTRSSAEITCDLTVINAFYIHWYLHQEGKAPQRLLYYDVSNSKDVLESGLSPG KYYTHTPRRWSWILILRNLIENDSGVYYCATWDRGNPKTHYYKKLFGSGTTLVVTDKQLD ADVSPKPTIFLPSIAETKLQKAGTYLCLLEKFFPDVIKIHWQEKKSNTILGSQEGNTMKT NDTYMKFSWLTVPEESLDKEHRCIVRHENNKNGVDQEIIFPPIK
Phosphoantigen-induced inside-out stabilization of butyrophilin receptor complexes drives dimerization-dependent gamma delta TCR activation. Zhu, Y., Gao, W., Zheng, J. et al. Immunity (2025) 58:1646-1659.e5. DOI 10.1016/j.immuni.2025.04.012 · PubMed
Other PDB entries of the same protein (UniProt Q6PJ56 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8ZD4 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.