Cryo-EM structure of ectodomains of HBMBPP-BTN2A1-BTN3A1 complex. Determined by electron microscopy at 3.67 Å resolution. Released 30 Apr 2025.
Explore 8ZAB in 3D Show helices and sheets RCSB PDB PDBe
8ZAB contains 19 α-helices and 100 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 | 4 | 1 | 1 |
| β-strand | 11-14 | 4 | 2 |
| β-strand | 15 | 1 | 3 |
| β-strand | 17 | 1 | 3 |
| β-strand | 25 | 1 | 1 |
| β-strand | 36-40 | 5 | 2 |
| β-strand | 48-51 | 4 | 2 |
| β-strand | 54-55 | 2 | 2 |
| α-helix | 57-59 | 3 | |
| β-strand | 70 | 1 | 4 |
| α-helix | 72-77 | 6 | |
| β-strand | 82 | 1 | 4 |
| β-strand | 93-98 | 6 | 2 |
| β-strand | 100-101 | 2 | 5 |
| β-strand | 104-105 | 2 | 5 |
| β-strand | 108-115 | 8 | 2 |
| β-strand | 116 | 1 | 6 |
| β-strand | 122-129 | 8 | 7 |
| β-strand | 132-138 | 7 | 7 |
| β-strand | 139-142 | 4 | 8 |
| β-strand | 143 | 1 | 6 |
| α-helix | 145-146 | 2 | |
| β-strand | 147-151 | 5 | 9 |
| β-strand | 157 | 1 | 9 |
| β-strand | 161-162 | 2 | 7 |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 8 |
| β-strand | 173-175 | 3 | 8 |
| β-strand | 177-181 | 5 | 7 |
| β-strand | 189-195 | 7 | 9 |
| β-strand | 200-208 | 9 | 9 |
| α-helix | 210-212 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 10 |
| β-strand | 11-14 | 4 | 11 |
| β-strand | 19-25 | 7 | 10 |
| β-strand | 36-40 | 5 | 11 |
| β-strand | 46-50 | 5 | 11 |
| β-strand | 55 | 1 | 11 |
| β-strand | 68-71 | 4 | 10 |
| β-strand | 79-84 | 6 | 10 |
| β-strand | 93-99 | 7 | 11 |
| β-strand | 101 | 1 | 12 |
| β-strand | 104 | 1 | 12 |
| β-strand | 109-115 | 7 | 11 |
| β-strand | 116 | 1 | 13 |
| β-strand | 122-128 | 7 | 9 |
| β-strand | 133-142 | 10 | 9 |
| β-strand | 143 | 1 | 13 |
| β-strand | 147-151 | 5 | 14 |
| β-strand | 161-162 | 2 | 9 |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 9 |
| α-helix | 172 | 1 | |
| β-strand | 173-178 | 6 | 9 |
| β-strand | 180 | 1 | 9 |
| β-strand | 190-194 | 5 | 14 |
| β-strand | 201-202 | 2 | 14 |
| β-strand | 205-208 | 4 | 7 |
| α-helix | 210-212 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 15 |
| β-strand | 11-14 | 4 | 16 |
| β-strand | 19-23 | 5 | 17 |
| β-strand | 24-26 | 3 | 15 |
| β-strand | 35-39 | 5 | 16 |
| β-strand | 46 | 1 | 18 |
| β-strand | 48-51 | 4 | 16 |
| β-strand | 54-55 | 2 | 16 |
| β-strand | 60 | 1 | 18 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-71 | 4 | 17 |
| α-helix | 75-77 | 3 | |
| β-strand | 80-84 | 5 | 17 |
| α-helix | 89-91 | 3 | |
| β-strand | 93-101 | 9 | 16 |
| β-strand | 104-115 | 12 | 16 |
| β-strand | 116 | 1 | 19 |
| α-helix | 119-121 | 3 | |
| β-strand | 122-128 | 7 | 20 |
| β-strand | 133-142 | 10 | 20 |
| β-strand | 143 | 1 | 19 |
| β-strand | 147-151 | 5 | 21 |
| α-helix | 158-160 | 3 | |
| β-strand | 162-167 | 6 | 20 |
| β-strand | 173-181 | 9 | 20 |
| β-strand | 190-195 | 6 | 21 |
| β-strand | 200-202 | 3 | 21 |
| β-strand | 205 | 1 | 21 |
| α-helix | 210-212 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-14 | 4 | 22 |
| β-strand | 21-23 | 3 | 23 |
| β-strand | 34-39 | 6 | 24 |
| β-strand | 46 | 1 | 25 |
| β-strand | 48-52 | 5 | 24 |
| α-helix | 57-59 | 3 | |
| β-strand | 60 | 1 | 25 |
| α-helix | 62-64 | 3 | |
| β-strand | 70-71 | 2 | 23 |
| β-strand | 80-82 | 3 | 23 |
| α-helix | 89-91 | 3 | |
| β-strand | 95 | 1 | 26 |
| β-strand | 96-100 | 5 | 24 |
| β-strand | 105-107 | 3 | 24 |
| β-strand | 110 | 1 | 26 |
| β-strand | 112-115 | 4 | 22 |
| β-strand | 116 | 1 | 27 |
| α-helix | 117-121 | 5 | |
| β-strand | 122-129 | 8 | 28 |
| β-strand | 132-138 | 7 | 28 |
| β-strand | 142 | 1 | 29 |
| β-strand | 143 | 1 | 27 |
| β-strand | 147-151 | 5 | 30 |
| β-strand | 157 | 1 | 30 |
| β-strand | 162-164 | 3 | 28 |
| β-strand | 167 | 1 | 29 |
| β-strand | 173 | 1 | 29 |
| β-strand | 176-181 | 6 | 28 |
| β-strand | 188-194 | 7 | 30 |
| β-strand | 201-207 | 7 | 30 |
| α-helix | 210-212 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Butyrophilin subfamily 3 member A1 | C, D | protein | 213 | Homo sapiens | O00481 (AlphaFold model) |
| Butyrophilin subfamily 2 member A1 | E, G | protein | 214 | Homo sapiens | Q7KYR7 (AlphaFold model) |
>8ZAB_1 Butyrophilin subfamily 3 member A1 (chains C, D) QFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQ SAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSD LHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVI MRGSSGEGVSCTIRSSLLGLEKTASISIADPFF
>8ZAB_2 Butyrophilin subfamily 2 member A1 (chains E, G) QFIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQ MEEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCYFQEGRSYDEAILHLVVAGLGSK PLISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVAPALKEVSMPDADGLFMVTTAVI IRDKSVRNMSCSINNTLLGQKKESVIFIPESFMP
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 O00481 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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