8UTB: Alpha7-nicotinic acetylcholine receptor

Alpha7-nicotinic acetylcholine receptor bound to epibatidine and NS-1738. Determined by electron microscopy at 2.3 Å resolution. Released 21 Feb 2024.

Method: Electron microscopy
Resolution: 2.3 Å
Organisms: Homo sapiens, Escherichia coli
Chains: 5
Atoms: 16,335
Mol. weight: 351.66 kDa
Ligands: POV, 9Z9, EPJ, NAG
Released: 21 Feb 2024

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

Secondary structure: helices and β-sheets

8UTB contains 75 α-helices and 75 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.

Chains A, B, C, D and E: 15 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	2-10	9
α-helix	27	1
β-strand	28-43	16	1
β-strand	48-60	13	1
β-strand	76-79	4	1
β-strand	89-91	3	2
β-strand	94	1	1
β-strand	102	1	1
α-helix	103-104	2
α-helix	106	1
β-strand	107-110	4	1
β-strand	114-117	4	1
β-strand	120-126	7	1
β-strand	138-147	10	2
β-strand	155-159	5	1
α-helix	161-162	2
β-strand	163	1	1
β-strand	173-177	5	2
β-strand	180-187	8	2
β-strand	190-205	16	2
α-helix	208-210	3
α-helix	211-215	5
α-helix	216-226	11
α-helix	227-229	3
α-helix	238-259	22
α-helix	270-295	26
α-helix	306-310	5
α-helix	311-316	6
α-helix	317-319	3
α-helix	409-458	50

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Neuronal acetylcholine receptor subunit alpha-7,Soluble cytochrome b562 fusion	A, B, C, D, E	protein	599	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P36544 (AlphaFold model)

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

>8UTB_1 Neuronal acetylcholine receptor subunit alpha-7,Soluble cytochrome b562 fusion (chains A, B, C, D, E)
EFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWT
DHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPP
GIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPG
KRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKIS
LGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPD
GGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLACGRMACAGAMADLEDN
WETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFD
ILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLSPTHDEHLLHGGQPPEGDPD
LAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPN
FVEAVSKDFAWSHPQFEKGGGSGGGSGGSSAWSHPQFEKGSGEGRGSLLTCGDVEENPG

Ligands and cofactors

ID	Name	Formula	Copies
POV	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…	C42 H82 N O8 P	5
9Z9	(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en	C34 H56 O5	5
EPJ	Epibatidine	C11 H13 Cl N2	5
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5
XG3	N-(5-chloro-2-hydroxyphenyl)-N'-[2-chloro-5-(trifluoromethyl)phenyl]urea	C14 H9 Cl2 F3 N2 O2	5

Primary citation

Structural mechanisms of alpha 7 nicotinic receptor allosteric modulation and activation. Burke, S.M., Avstrikova, M., Noviello, C.M. et al. Cell (2024) 187:1160-1176.e21. DOI 10.1016/j.cell.2024.01.032 · PubMed

Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y

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