5HM7: Butyrophilin subfamily 3 member A1

The Intracellular domain of Butyrophilin 3A1 protein. Determined by X-ray diffraction at 1.93 Å resolution. Released 26 Jul 2017.

Method: X-ray diffraction
Resolution: 1.93 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,439
Mol. weight: 57.89 kDa
Ligands: MG
Released: 26 Jul 2017

Explore 5HM7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HM7 contains 11 α-helices and 34 β-strands across 2 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: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	278-290	13
α-helix	295-306	12
β-strand	308-309	2	1
β-strand	314	1	2
α-helix	316-318	3
β-strand	323-325	3	1
β-strand	331-334	4	1
β-strand	353-355	3	3
β-strand	356	1	2
β-strand	360	1	3
β-strand	364-370	7	1
β-strand	377-383	7	3
α-helix	396-398	3
β-strand	400-406	7	3
β-strand	410-413	4	3
β-strand	419-420	2	3
β-strand	429-435	7	1
β-strand	440-445	6	1
β-strand	451-455	5	1
β-strand	464-469	6	3
α-helix	477	1
β-strand	478-480	3	1
α-helix	481-482	2

Chain B: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	295-306	12
β-strand	308-309	2	4
β-strand	314	1	5
α-helix	316-318	3
β-strand	323-325	3	4
β-strand	331-334	4	4
β-strand	353-355	3	6
β-strand	356	1	5
β-strand	360	1	6
β-strand	364-370	7	4
β-strand	377-383	7	6
α-helix	396-398	3
β-strand	400-406	7	6
β-strand	410-413	4	6
β-strand	419-420	2	6
β-strand	429-435	7	4
β-strand	440-445	6	4
β-strand	451-455	5	4
β-strand	464-469	6	6
α-helix	477	1
β-strand	478-480	3	4
α-helix	481-482	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Butyrophilin subfamily 3 member A1	A, B	protein	244	Homo sapiens	O00481 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5HM7_1 Butyrophilin subfamily 3 member A1 (chains A, B)
MGQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAY
NEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCES
FISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRT
NLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALT
ICPA

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2

Water and common crystallization additives (BME, GOL) are not listed.

Primary citation

Phosphoantigen-induced conformational change of butyrophilin 3A1 (BTN3A1) and its implication on V gamma 9V delta 2 T cell activation. Gu, S., Sachleben, J.R., Boughter, C.T. et al. Proc Natl Acad Sci U S A (2017) 114:E7311-E7320. DOI 10.1073/pnas.1707547114 · PubMed

Other PDB entries of the same protein (UniProt O00481 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ITA 1.2 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 mutant
6ISM 1.25 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 mutant
8IZE 1.4 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 in complex with 4-HMBPP
4N7I 1.4 Å, Crystal Structure of Intracellular B30.2 Domain of BTN3A1
4N7U 1.46 Å, Crystal Structure of Intracellular B30.2 Domain of BTN3A1 in Complex with CHDMAPP
5LYG 1.6 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 bound to malonate
8IZG 1.6 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 in complex with 5-HMBPP
5LYK 1.7 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 bound to citrate
8IXV 1.72 Å, Crystal structure of intracellular B30.2 domain of BTN3A in complex with 2Cl-HMBPP
4K55 1.91 Å, Structure of the extracellular domain of butyrophilin BTN3A1 in complex with…
4F80 1.94 Å, Crystal Structure of the human BTN3A1 ectodomain
5ZXK 1.96 Å, Crystal structure of intracellular B30.2 domain of BTN3A1 in complex with HMBPP

Browse structure collections

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