8VC7: Human BTN2A1 ectodomain

Crystal Structure of Human BTN2A1 ectodomain in complex with Antagonist 2A1.9 Fab. Determined by X-ray diffraction at 2.76 Å resolution. Released 18 Dec 2024.

Method: X-ray diffraction
Resolution: 2.76 Å
Organism: Homo sapiens
Chains: 6
Atoms: 9,797
Mol. weight: 148.75 kDa
Ligands: NAG
Released: 18 Dec 2024

Explore 8VC7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VC7 contains 47 α-helices and 134 β-strands across 6 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, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	18
β-strand	11-14	4	19
β-strand	20-26	7	18
β-strand	30	1	20
β-strand	32	1	20
β-strand	34-39	6	19
β-strand	46-50	5	19
β-strand	54-55	2	19
α-helix	56	1
β-strand	63-68	6	18
β-strand	71-76	6	18
α-helix	81-83	3
β-strand	86-91	6	19
β-strand	98-99	2	19
β-strand	103-107	5	19
β-strand	112	1	21
α-helix	113-114	2
β-strand	115-119	5	22
α-helix	120-122	3
α-helix	123-126	4
β-strand	130-140	11	22
β-strand	141	1	21
β-strand	145-151	7	23
β-strand	155	1	23
β-strand	160-164	5	22
α-helix	165-168	4
β-strand	174-183	10	22
α-helix	184-188	5
β-strand	192-199	8	23
β-strand	206-211	6	23

Chain B: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	24
β-strand	14-15	2	25
β-strand	21-28	8	24
α-helix	32-34	3
β-strand	35-42	8	26
β-strand	49-55	7	26
β-strand	60-63	4	26
β-strand	71-76	6	24
β-strand	81-86	6	24
α-helix	91-93	3
β-strand	95-103	9	26
β-strand	114-115	2	26
β-strand	119-121	3	26
β-strand	122-123	2	25
β-strand	129	1	27
α-helix	130-131	2
β-strand	132-136	5	28
β-strand	147-157	11	28
β-strand	158	1	27
β-strand	163-166	4	29
α-helix	167-169	3
β-strand	171	1	29
β-strand	175-177	3	28
α-helix	178-180	3
β-strand	181-182	2	28
β-strand	188-197	10	28
α-helix	198-201	4
β-strand	206-212	7	29
α-helix	213-215	3
β-strand	217-223	7	29

Chain C: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	12
β-strand	11-14	4	13
β-strand	19-25	7	12
β-strand	35-39	5	13
β-strand	46	1	14
β-strand	48-51	4	13
β-strand	54-55	2	13
α-helix	57-59	3
β-strand	60	1	14
α-helix	62-64	3
β-strand	68-71	4	12
α-helix	75-77	3
β-strand	79-84	6	12
α-helix	85	1
α-helix	89-91	3
β-strand	93-101	9	13
β-strand	104-115	12	13
β-strand	116	1	15
α-helix	119-121	3
β-strand	122-129	8	16
β-strand	132-142	11	16
β-strand	143	1	15
β-strand	147-151	5	17
β-strand	157-158	2	17
α-helix	159-160	2
β-strand	162-167	6	16
α-helix	172	1
β-strand	173-181	9	16
β-strand	188-195	8	17
β-strand	200-207	8	17
α-helix	210-212	3

Chain D: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-8	4	1
β-strand	11-14	4	2
β-strand	20-26	7	1
β-strand	34-39	6	2
β-strand	46-50	5	2
β-strand	54-55	2	2
α-helix	56	1
β-strand	63-68	6	1
β-strand	71-76	6	1
α-helix	81-83	3
β-strand	86-91	6	2
β-strand	98-99	2	2
β-strand	103-107	5	2
β-strand	112	1	3
α-helix	113-114	2
β-strand	115-119	5	4
α-helix	120-122	3
α-helix	123-128	6
β-strand	130-140	11	4
β-strand	141	1	3
β-strand	145-151	7	5
β-strand	154-155	2	5
β-strand	160-164	5	4
α-helix	165-168	4
β-strand	174-183	10	4
α-helix	184-188	5
β-strand	192-199	8	5
β-strand	206-211	6	5

Chain E: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	30
β-strand	11-14	4	31
β-strand	19-25	7	30
β-strand	35-39	5	31
β-strand	46	1	32
β-strand	48-51	4	31
β-strand	54-55	2	31
α-helix	57-59	3
β-strand	60	1	32
α-helix	62-64	3
β-strand	68-74	7	30
α-helix	75-77	3
β-strand	79-84	6	30
α-helix	85	1
α-helix	89-91	3
β-strand	93-101	9	31
β-strand	104-115	12	31
β-strand	116	1	33
α-helix	119-121	3
β-strand	122-129	8	34
β-strand	132-142	11	34
β-strand	143	1	33
α-helix	145-146	2
β-strand	147-151	5	35
β-strand	157-158	2	35
α-helix	159-160	2
β-strand	162-167	6	34
α-helix	172	1
β-strand	173-181	9	34
β-strand	188-195	8	35
β-strand	200-207	8	35
α-helix	210-212	3

Chain J: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	6
β-strand	14-15	2	7
β-strand	21-28	8	6
α-helix	32-34	3
β-strand	35-42	8	8
β-strand	48-54	7	8
β-strand	61-63	3	8
β-strand	71-76	6	6
β-strand	81-86	6	6
α-helix	91-93	3
β-strand	95-103	9	8
β-strand	114-115	2	8
β-strand	119-121	3	8
β-strand	122-123	2	7
β-strand	129	1	9
α-helix	130-131	2
β-strand	132-136	5	10
β-strand	147-157	11	10
β-strand	158	1	9
β-strand	163-166	4	11
α-helix	167-169	3
β-strand	171	1	11
β-strand	175-177	3	10
α-helix	178-180	3
β-strand	181-182	2	10
β-strand	188-197	10	10
α-helix	198-201	4
β-strand	207-212	6	11
α-helix	213-215	3
β-strand	217-222	6	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Human IgG1 Fragment Antibody Light Chain	A, D	protein	215	Homo sapiens
Human IgG1 Fragment Antibody Heavy Chain	B, J	protein	233	Homo sapiens
Butyrophilin subfamily 2 member A1	C, E	protein	231	Homo sapiens	Q7KYR7 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>8VC7_1 Human IgG1 Fragment Antibody Light Chain (chains A, D)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSSSSLITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (B, J), FASTA

>8VC7_2 Human IgG1 Fragment Antibody Heavy Chain (chains B, J)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNLYSSSIHWVRQAPGKGLEWVAYIYPSSGY
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARYYYTRGYPDGMDYWGQGTL
VTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPA
VLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 3 (C, E), FASTA

>8VC7_3 Butyrophilin subfamily 2 member A1 (chains C, E)
ADLQFIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERT
EEQMEEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCYFQEGRSYDEAILHLVVAGL
GSKPLISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVAPALKEVSMPDADGLFMVTT
AVIIRDKSVRNMSCSINNTLLGQKKESVIFIPESFMPSVSPSGSGLEVLFQ

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

Primary citation

Mapping the extracellular molecular architecture of the pAg-signaling complex with alpha-Butyrophilin antibodies. Ramesh, A., Roy, S., Slezak, T. et al. Sci Rep (2025) 15:12162-12162. DOI 10.1038/s41598-025-94347-w · 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
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…
8ZJX 3.35 Å, Cryo-EM structure of the full length pAg-bound BTN2A1-BTN3A1-BTN3A2 in complex with…

Browse structure collections

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