8DFY: Human BTN2A1 Ectodomain

Crystal structure of Human BTN2A1 Ectodomain. Determined by X-ray diffraction at 3.55 Å resolution. Released 5 Jul 2023.

Method: X-ray diffraction
Resolution: 3.55 Å
Organism: Homo sapiens
Chains: 5
Atoms: 8,993
Mol. weight: 134.32 kDa
Ligands: NAG
Released: 5 Jul 2023

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

Secondary structure: helices and β-sheets

8DFY contains 41 α-helices and 115 β-strands across 5 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	3-5	3	1
β-strand	11-14	4	2
β-strand	19-23	5	3
β-strand	24-26	3	1
β-strand	35-39	5	2
β-strand	46	1	4
β-strand	48-51	4	2
β-strand	54-55	2	2
β-strand	60	1	4
α-helix	62-64	3
β-strand	68-74	7	3
α-helix	75-77	3
β-strand	79-84	6	3
α-helix	89-91	3
β-strand	93-101	9	2
β-strand	104-115	12	2
β-strand	116	1	5
α-helix	119-121	3
β-strand	122-129	8	6
β-strand	132-142	11	6
β-strand	143	1	5
α-helix	145-146	2
β-strand	147-151	5	7
β-strand	157-158	2	7
β-strand	162-167	6	6
α-helix	172	1
β-strand	173-181	9	6
β-strand	188-195	8	7
β-strand	200-207	8	7
α-helix	210-212	3

Chain B: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	8
β-strand	11-14	4	9
β-strand	19-23	5	10
β-strand	24-26	3	8
β-strand	35-39	5	9
β-strand	46	1	11
β-strand	48-51	4	9
β-strand	54-55	2	9
α-helix	57-59	3
β-strand	60	1	11
α-helix	62-64	3
β-strand	68-71	4	10
α-helix	75-77	3
β-strand	80-84	5	10
α-helix	89-91	3
β-strand	93-101	9	9
β-strand	104-115	12	9
β-strand	116	1	12
α-helix	119-121	3
β-strand	122-129	8	13
β-strand	132-142	11	13
β-strand	143	1	12
α-helix	145-146	2
β-strand	147-151	5	14
α-helix	156	1
β-strand	157-158	2	14
α-helix	159-160	2
β-strand	162-167	6	13
α-helix	172	1
β-strand	173-181	9	13
β-strand	188-195	8	14
β-strand	200-207	8	14
α-helix	210-212	3

Chain C: 8 helices, 23 β-strands

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
α-helix	57-59	3
β-strand	60	1	18
α-helix	62-64	3
β-strand	68-74	7	17
α-helix	75-77	3
β-strand	79-84	6	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	122-129	8	20
β-strand	132-142	11	20
β-strand	143	1	19
α-helix	145-146	2
β-strand	147-151	5	21
β-strand	157-158	2	21
β-strand	162-167	6	20
α-helix	172	1
β-strand	173-181	9	20
β-strand	188-195	8	21
β-strand	200-207	8	21
α-helix	210-212	3

Chain D: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	22
β-strand	11-14	4	23
β-strand	19-23	5	24
β-strand	24-26	3	22
β-strand	33-39	7	23
β-strand	46	1	25
β-strand	48-52	5	23
β-strand	54-55	2	23
α-helix	57-59	3
β-strand	60	1	25
α-helix	62-64	3
β-strand	68-74	7	24
α-helix	75-77	3
β-strand	79-84	6	24
α-helix	89-91	3
β-strand	93-101	9	23
β-strand	104-115	12	23
β-strand	116	1	26
α-helix	119-121	3
β-strand	122-129	8	27
β-strand	132-142	11	27
β-strand	143	1	26
α-helix	145-146	2
β-strand	147-151	5	28
β-strand	157-158	2	28
β-strand	162-167	6	27
α-helix	172	1
β-strand	173-181	9	27
β-strand	188-195	8	28
β-strand	200-207	8	28
α-helix	210-212	3

Chain E: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	29
β-strand	11-14	4	30
β-strand	19-23	5	31
β-strand	24-26	3	29
β-strand	35-39	5	30
β-strand	46	1	32
β-strand	48-51	4	30
β-strand	54-55	2	30
α-helix	57-59	3
β-strand	60	1	32
α-helix	62-64	3
β-strand	68-71	4	31
α-helix	75-77	3
β-strand	80-84	5	31
α-helix	89-91	3
β-strand	93-101	9	30
β-strand	104-115	12	30
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
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Butyrophilin subfamily 2 member A1	A, B, C, D, E	protein	226	Homo sapiens	Q7KYR7 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>8DFY_1 Butyrophilin subfamily 2 member A1 (chains A, B, C, D, E)
ETGQFIVVGPTDPILATVGENTTLRCHLSPEKNAEDMEVRWFRSQFSPAVFVYKGGRERT
EEQMEEYRGRTTFVSKDISRGSVALVIHNITAQENGTYRCYFQEGRSYDEAILHLVVAGL
GSKPLISMRGHEDGGIRLECISRGWYPKPLTVWRDPYGGVAPALKEVSMPDADGLFMVTT
AVIIRDKSVRNMSCSINNTLLGQKKESVIFIPESFMPSVSHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	12

Primary citation

Vgamma9-Vdelta2 T cells recognize butyrophilin 2A1 and 3A1 heteromers. Fulford, T.S., Soliman, C., Castle, R.G. et al. To be published.

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…

Browse structure collections

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