8ZJZ: Butyrophilin subfamily 2 member A1

Cryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3A3 complex. Determined by electron microscopy at 3.8 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 15,540
Mol. weight: 221.05 kDa
Ligands: H6P
Released: 26 Nov 2025

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

Secondary structure: helices and β-sheets

8ZJZ contains 32 α-helices and 154 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: 7 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	33	1	1
β-strand	39-41	3	2
β-strand	47-51	5	3
β-strand	52	1	1
β-strand	63-67	5	2
β-strand	76-78	3	2
β-strand	79	1	4
β-strand	82	1	4
β-strand	96-99	4	3
β-strand	108-112	5	3
α-helix	117-119	3
β-strand	121-128	8	2
β-strand	134-142	9	2
β-strand	144	1	5
β-strand	150-153	4	6
β-strand	162-170	9	6
β-strand	171	1	5
β-strand	175-179	5	7
α-helix	186-188	3
β-strand	190	1	6
β-strand	195	1	6
β-strand	201-208	8	6
β-strand	216-222	7	7
β-strand	229-230	2	7
β-strand	233-235	3	7
α-helix	251-321	71
β-strand	325-327	3	8
β-strand	332	1	9
α-helix	334-336	3
β-strand	341-343	3	8
β-strand	349-352	4	8
β-strand	374-376	3	10
β-strand	377	1	9
β-strand	381	1	10
β-strand	385-391	7	8
β-strand	398-404	7	10
β-strand	421-427	7	10
β-strand	430-433	4	10
β-strand	440	1	10
β-strand	450-455	6	8
α-helix	456-458	3
β-strand	460-465	6	8
β-strand	470-474	5	8
α-helix	475-477	3
β-strand	484-489	6	10
β-strand	493	1	8
β-strand	497-499	3	8
α-helix	500-503	4

Chain B: 6 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	31-33	3	11
β-strand	39-42	4	12
β-strand	47-51	5	13
β-strand	52-54	3	11
β-strand	63-67	5	12
β-strand	76-79	4	12
α-helix	90-92	3
β-strand	96-99	4	13
β-strand	108-112	5	13
α-helix	117-119	3
β-strand	121-128	8	12
β-strand	133-143	11	12
β-strand	144	1	14
α-helix	147-149	3
β-strand	150-153	4	15
β-strand	162-170	9	15
β-strand	171	1	14
β-strand	176-179	4	16
β-strand	185-186	2	16
β-strand	190-195	6	15
β-strand	201-208	8	15
β-strand	217-221	5	16
β-strand	230-234	5	16
α-helix	251-320	70
β-strand	325-327	3	8
β-strand	341-343	3	8
β-strand	349-352	4	8
β-strand	374-375	2	17
β-strand	381	1	17
β-strand	385-391	7	8
β-strand	398-404	7	17
α-helix	417-419	3
β-strand	421-427	7	17
β-strand	430-432	3	17
β-strand	440-441	2	17
β-strand	449-455	7	8
β-strand	460-465	6	8
β-strand	470-474	5	8
β-strand	484-490	7	17
β-strand	497-499	3	8
α-helix	501-503	3
β-strand	516-517	2	8

Chain E: 7 helices, 39 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	18
β-strand	40-43	4	19
β-strand	50-53	4	20
β-strand	55	1	18
β-strand	66-69	4	19
β-strand	75-78	4	19
β-strand	79-80	2	21
β-strand	83-84	2	21
α-helix	91-93	3
β-strand	97-100	4	20
β-strand	108-113	6	20
β-strand	122-129	8	19
β-strand	134-144	11	19
β-strand	145	1	22
β-strand	151-158	8	23
β-strand	161-171	11	23
β-strand	172	1	22
β-strand	176-181	6	24
β-strand	186-187	2	24
β-strand	190-191	2	23
α-helix	192-194	3
β-strand	195-196	2	23
β-strand	202-210	9	23
β-strand	218-223	6	24
β-strand	230-237	8	24
α-helix	246-321	76
α-helix	331-336	6
β-strand	344	1	25
α-helix	346-348	3
β-strand	353-355	3	26
β-strand	362-364	3	26
β-strand	384	1	27
β-strand	386	1	25
β-strand	390	1	28
β-strand	397-400	4	29
β-strand	407-412	6	27
α-helix	427-429	3
β-strand	431-437	7	27
β-strand	441-444	4	27
β-strand	450-452	3	27
β-strand	460-463	4	29
β-strand	472-476	5	29
β-strand	482-486	5	29
α-helix	494	1
β-strand	495	1	28
β-strand	496-500	5	27

Chain F: 12 helices, 38 β-strands

Element	Residues	Length	Sheet
β-strand	32	1	30
β-strand	40-42	3	31
β-strand	48-51	4	32
β-strand	55	1	30
β-strand	66-69	4	31
β-strand	74-78	5	31
β-strand	79-80	2	33
β-strand	83-84	2	33
α-helix	91-93	3
β-strand	97-99	3	32
α-helix	103-106	4
β-strand	110-113	4	32
β-strand	122-127	6	31
β-strand	137-143	7	31
β-strand	145	1	34
α-helix	147-150	4
β-strand	151-158	8	24
β-strand	161-171	11	24
β-strand	172	1	34
β-strand	176-181	6	23
α-helix	185	1
β-strand	186-187	2	23
α-helix	188	1
β-strand	190-191	2	24
α-helix	192-194	3
β-strand	202-210	9	24
β-strand	218-223	6	23
β-strand	230-236	7	23
α-helix	240-242	3
α-helix	245-318	74
α-helix	326-336	11
β-strand	339	1	35
β-strand	344-345	2	36
β-strand	353-355	3	37
β-strand	362-364	3	37
α-helix	371-373	3
β-strand	383-386	4	36
β-strand	390	1	36
β-strand	394-400	7	35
β-strand	407-413	7	36
α-helix	426-428	3
β-strand	430-436	7	36
β-strand	440-443	4	36
β-strand	449-450	2	36
β-strand	460-465	6	35
β-strand	470-475	6	35
β-strand	481-485	5	35
β-strand	494-499	6	36
β-strand	509-510	2	35
α-helix	511-512	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Butyrophilin subfamily 2 member A1	A, B	protein	492	Homo sapiens	Q7KYR7 (AlphaFold model)
Butyrophilin subfamily 3 member A3	E	protein	482	Homo sapiens	O00478 (AlphaFold model)
Butyrophilin subfamily 3 member A1	F	protein	484	Homo sapiens	O00481 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8ZJZ_1 Butyrophilin subfamily 2 member A1 (chains A, B)
FIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERTEEQM
EEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCYFQEGRSYDEAILHLVVAGLGSKP
LISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVAPALKEVSMPDADGLFMVTTAVII
RDKSVRNMSCSINNTLLGQKKESVIFIPESFMPSVSPCAVALPIIVVILMIPIAVCIYWI
NKLQKEKKILSGEKEFERETREIALKELEKERVQKEEELQVKEKLQEELRWRRTFLHAVD
VVLDPDTAHPDLFLSEDRRSVRRCPFRHLGESVPDNPERFDSQPCVLGRESFASGKHYWE
VEVENVIEWTVGVCRDSVERKGEVLLIPQNGFWTLEMHKGQYRAVSSPDRILPLKESLCR
VGVFLDYEAGDVSFYNMRDRSHIYTCPRSAFSVPVRPFFRLGCEDSPIFICPALTGANGV
TVPEEGLTLHRV

Sequence of entity 2 (E), FASTA

>8ZJZ_2 Butyrophilin subfamily 3 member A3 (chains E)
QFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELRWVSSSLRQVVNVYADGKEVEDRQ
SAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSD
LHIEVKGYEDGGIHLECRSTGWYPQPQIKWSDTKGENIPAVEAPVVADGVGLYAVAASVI
MRGSSGGGVSCIIRNSLLGLEKTASISIADPFFRSAQPWIAALAGTLPISLLLLAGASYF
LWRQQKEKIALSRETEREREMKEMGYAATEQEISLREKLQEELKWRKIQYMARGEKSLAY
HEWKMALFKPADVILDPDTANAILLVSEDQRSVQRAEEPRDLPDNPERFEWRYCVLGCEN
FTSGRHYWEVEVGDRKEWHIGVCSKNVERKKGWVKMTPENGYWTMGLTDGNKYRALTEPR
TNLKLPEPPRKVGIFLDYETGEISFYNATDGSHIYTFPHASFSEPLYPVFRILTLEPTAL
TI

Sequence of entity 3 (F), FASTA

>8ZJZ_3 Butyrophilin subfamily 3 member A1 (chains F)
QFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQ
SAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSD
LHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVI
MRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYF
LWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAY
NEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCES
FISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRT
NLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALT
ICPA

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 Q7KYR7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8IGT 1.56 Å, Crystal Structure of Intracellular B30.2 Domain of BTN2A1
8DFW 2.1 Å, Crystal Structure of Human BTN2A1 in Complex With Vgamma9-Vdelta2 T Cell Receptor
8JYE 2.18 Å, Crystal Structure of Intracellular B30.2 Domain of BTN3A1 and BTN2A1 in Complex with HMBPP
8JYC 2.29 Å, Crystal Structure of Intracellular B30.2 Domain of BTN3A1 and BTN2A1 in Complex with DMAPP
8VC7 2.76 Å, Crystal Structure of Human BTN2A1 ectodomain in complex with Antagonist 2A1.9 Fab
8ZHR 3.0 Å, Cryo-EM structure of the full-length pAg-bound BTN2A1-BTN3A1-BTN3A2 complex
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
9II6 3.27 Å, Cryo-EM structure of the intracellular domains of BTN2A1-BTN3A1-BTN3A3
9JQ6 3.34 Å, Cryo-EM structure of BTN2A1 in complex with antagonist antibody TH002
9JQP 3.34 Å, Cryo-EM structure of the HMBPP-primed BTN3A1-BTN3A2-BTN2A1 in complex with agonist…

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