8ZHR: Butyrophilin subfamily 3 member A2

Cryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3A2 complex. Determined by electron microscopy at 3.0 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,005
Mol. weight: 214.55 kDa
Ligands: H6P
Released: 26 Nov 2025

Explore 8ZHR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8ZHR contains 43 α-helices and 141 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.

Chain A: 13 helices, 42 β-strands

Element	Residues	Length	Sheet
β-strand	31-33	3	22
β-strand	39-41	3	23
β-strand	47-51	5	24
β-strand	52-54	3	22
β-strand	63-67	5	23
β-strand	74	1	25
β-strand	76-79	4	23
β-strand	82-83	2	23
α-helix	85-87	3
β-strand	88	1	25
β-strand	96-102	7	24
α-helix	103-105	3
β-strand	107-112	6	24
α-helix	117-119	3
β-strand	121-129	9	23
β-strand	132-142	11	23
β-strand	144	1	26
α-helix	147-149	3
β-strand	150-157	8	27
β-strand	160-170	11	27
β-strand	171	1	26
β-strand	175-177	3	28
α-helix	186-188	3
β-strand	190-195	6	27
β-strand	201-208	8	27
β-strand	216-217	2	29
β-strand	220-222	3	28
β-strand	229-230	2	28
β-strand	234-235	2	29
α-helix	238-240	3
α-helix	243-245	3
α-helix	247-321	75
β-strand	325-327	3	12
β-strand	332	1	30
β-strand	341-343	3	12
α-helix	344	1
β-strand	349-352	4	12
β-strand	374-376	3	31
β-strand	377	1	30
β-strand	381	1	31
β-strand	385-391	7	12
β-strand	398-404	7	31
α-helix	417-419	3
β-strand	421-427	7	31
β-strand	430-433	4	31
β-strand	440	1	31
β-strand	449-455	7	12
β-strand	460-465	6	12
β-strand	470-474	5	12
α-helix	475-477	3
β-strand	484-490	7	31
β-strand	497-500	4	12
α-helix	501-503	3
α-helix	510-512	3
β-strand	516-517	2	12

Chain B: 12 helices, 40 β-strands

Element	Residues	Length	Sheet
β-strand	32-33	2	6
β-strand	39-41	3	7
β-strand	47-53	7	6
β-strand	63-67	5	7
β-strand	74	1	8
β-strand	76-79	4	7
β-strand	82-83	2	7
β-strand	88	1	8
β-strand	96-98	3	6
α-helix	103-105	3
β-strand	107-112	6	6
α-helix	117-119	3
β-strand	121-129	9	7
β-strand	132-142	11	7
β-strand	144	1	9
α-helix	147-149	3
β-strand	150-156	7	10
β-strand	161-170	10	10
β-strand	171	1	9
β-strand	175-179	5	11
β-strand	185-186	2	11
α-helix	187-188	2
β-strand	190-195	6	10
α-helix	200	1
β-strand	201-209	9	10
β-strand	216-222	7	11
β-strand	229-235	7	11
α-helix	238-240	3
α-helix	243-245	3
α-helix	246-322	77
β-strand	326-327	2	12
β-strand	332	1	13
β-strand	341-343	3	12
β-strand	349-352	4	12
β-strand	374-376	3	14
β-strand	377	1	13
β-strand	381	1	14
β-strand	385-391	7	12
β-strand	398-404	7	14
α-helix	417-419	3
β-strand	421-427	7	14
β-strand	430-433	4	14
α-helix	437-439	3
β-strand	440	1	14
β-strand	449-455	7	12
β-strand	460-465	6	12
β-strand	470-474	5	12
α-helix	475-477	3
β-strand	484-490	7	14
β-strand	497-499	3	12
α-helix	501-503	3
β-strand	516-517	2	12

Chain E: 9 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	33-34	2	1
β-strand	40-43	4	2
β-strand	48-54	7	1
β-strand	64-69	6	2
β-strand	75-80	6	2
β-strand	83-84	2	2
α-helix	91-93	3
β-strand	97-100	4	1
α-helix	104-106	3
β-strand	108-113	6	1
α-helix	118-120	3
β-strand	122-129	8	2
β-strand	134-144	11	2
β-strand	145	1	3
α-helix	148-150	3
β-strand	151-156	6	4
β-strand	162-171	10	4
β-strand	172	1	3
β-strand	176-180	5	5
β-strand	186-187	2	5
α-helix	188	1
β-strand	190-191	2	4
α-helix	192-194	3
β-strand	202-210	9	4
α-helix	216-217	2
β-strand	218-224	7	5
β-strand	229-237	9	5
α-helix	239-242	4
α-helix	246-321	76

Chain F: 9 helices, 39 β-strands

Element	Residues	Length	Sheet
β-strand	32-34	3	15
β-strand	40-42	3	16
β-strand	48-52	5	17
β-strand	53-55	3	15
β-strand	64-69	6	16
β-strand	74-80	7	16
β-strand	83-84	2	16
β-strand	97-103	7	17
α-helix	104-106	3
β-strand	108-113	6	17
α-helix	118-120	3
β-strand	122-130	9	16
β-strand	133-143	11	16
β-strand	145	1	18
α-helix	148-150	3
β-strand	151-157	7	5
β-strand	162-171	10	5
β-strand	172	1	18
β-strand	176-180	5	4
β-strand	186-187	2	4
β-strand	190-191	2	5
α-helix	192-194	3
β-strand	195-196	2	5
β-strand	202-210	9	5
β-strand	218-224	7	4
β-strand	229-237	9	4
α-helix	239-242	4
α-helix	245-318	74
α-helix	326-336	11
β-strand	338-339	2	19
β-strand	344	1	20
β-strand	353-355	3	19
β-strand	361-364	4	19
β-strand	383-385	3	21
β-strand	386	1	20
β-strand	390	1	21
β-strand	394-400	7	19
β-strand	407-413	7	21
α-helix	426-428	3
β-strand	430-436	7	21
β-strand	440-443	4	21
β-strand	449-451	3	21
β-strand	459-465	7	19
β-strand	470-475	6	19
β-strand	481-485	5	19
β-strand	494-499	6	21
β-strand	508-510	3	19
α-helix	511-512	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Butyrophilin subfamily 3 member A2	E	protein	327	Homo sapiens	P78410 (AlphaFold model)
Butyrophilin subfamily 2 member A1	A, B	protein	534	Homo sapiens	Q7KYR7 (AlphaFold model)
Butyrophilin subfamily 3 member A1	F	protein	510	Homo sapiens	O00481 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>8ZHR_1 Butyrophilin subfamily 3 member A2 (chains E)
MDMRVPAQLLGLLLLWLSGARCQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKW
VSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCY
FQDGDFYEKALVELKVAALGSNLHVEVKGYEDGGIHLECRSTGWYPQPQIQWSNAKGENI
PAVEAPVVADGVGLYEVAASVIMRGGSGEGVSCIIRNSLLGLEKTASISIADPFFRSAQP
WIAALAGTLPILLLLLAGASYFLWRQQKEITALSSEIESEQEMKEMGYAATEREISLRES
LQEELKRKKIQYLTRGEESSSDTNKSA

Sequence of entity 2 (A, B), FASTA

>8ZHR_2 Butyrophilin subfamily 2 member A1 (chains A, B)
MDMRVPAQLLGLLLLWLSGARCQFIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRW
FRSQFSPAVFVYKGGRERTEEQMEEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCY
FQEGRSYDEAILHLVVAGLGSKPLISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVA
PALKEVSMPDADGLFMVTTAVIIRDKSVRNMSCSINNTLLGQKKESVIFIPESFMPSVSP
CAVALPIIVVILMIPIAVCIYWINKLQKEKKILSGEKEFERETREIALKELEKERVQKEE
ELQVKEKLQEELRWRRTFLHAVDVVLDPDTAHPDLFLSEDRRSVRRCPFRHLGESVPDNP
ERFDSQPCVLGRESFASGKHYWEVEVENVIEWTVGVCRDSVERKGEVLLIPQNGFWTLEM
HKGQYRAVSSPDRILPLKESLCRVGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVPVRP
FFRLGCEDSPIFICPALTGANGVTVPEEGLTLHRVGTHQSLGSSGMDYKDDDDK

Sequence of entity 3 (F), FASTA

>8ZHR_3 Butyrophilin subfamily 3 member A1 (chains F)
MDMRVPAQLLGLLLLWLSGARCQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKW
VSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCY
FQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENI
PTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQR
WIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVK
LLEELRWRSIQYASRGERHSAYNEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKE
PQDLPDNPERFNWHYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPE
NGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLD
VSFSEALYPVFRILTLEPTALTICPAGSSG

Ligands and cofactors

ID	Name	Formula	Copies
H6P	(2E)-4-hydroxy-3-methylbut-2-en-1-yl trihydrogen diphosphate	C5 H12 O8 P2	1

Primary citation

Phosphoantigen-driven dissociation of butyrophilin oligomers activates gamma delta T cells. Xin, W., Huang, B., Gao, W. et al. Cell Discov (2026) 12. DOI 10.1038/s41421-026-00911-7 · PubMed

Other PDB entries of the same protein (UniProt P78410 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4F8Q 2.38 Å, Crystal Structure of the Human BTN3A2 Ectodomain
9JQR 3.0 Å, Cryo-EM structure of the Vgamma9Vdelta2 TCR-engaged BTN3A1-BTN3A2-BTN2A1 complex
9IRD 3.2 Å, Cryo-EM structure of BTN2A1-BTN3A1-BTN3A2 mutant (BTN3A1 H381R, BTN2A1 R477A/T510A) in…
9JQQ 3.26 Å, Cryo-EM structure of the HMBPP-primed BTN3A1-BTN3A2-BTN2A1 complex
9JQP 3.34 Å, Cryo-EM structure of the HMBPP-primed BTN3A1-BTN3A2-BTN2A1 in complex with agonist…
8ZJX 3.35 Å, Cryo-EM structure of the full length pAg-bound BTN2A1-BTN3A1-BTN3A2 in complex with…
8ZK0 3.4 Å, Cryo-EM structure of the full length pAg-bound BTN2A1-BTN3A1-BTN3A2 in complex with…
9L1P 3.5 Å, Cryo-EM structure of the ICT01-BTN2A1/BTN3A1/BTN3A2 complex, local refinement
9KWE 3.7 Å, Cryo-EM structure of the ICT01-BTN3A1/BTN3A2 complex
9KWZ 3.7 Å, Cryo-EM structure of the ICT01-BTN2A1/BTN3A1/BTN3A2 complex
9L1O 3.7 Å, Cryo-EM structure of the ICT01-BTN3A1/BTN3A2 complex, local refinement
8ZK1 3.8 Å, Cryo-EM structure of BTN2A1-BTN3A1-BTN3A2 mutant complex (BTN3A1 H381R, BTN2A1…

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