7KOO: Alpha-7 nicotinic acetylcholine receptor

Alpha-7 nicotinic acetylcholine receptor bound to alpha-bungarotoxin in a resting state. Determined by electron microscopy at 3.0 Å resolution. Released 17 Mar 2021.

Method: Electron microscopy
Resolution: 3.0 Å
Organisms: Homo sapiens, Escherichia coli, Bungarus multicinctus
Chains: 10
Atoms: 18,915
Mol. weight: 364.94 kDa
Ligands: CA, NAG
Released: 17 Mar 2021

Explore 7KOO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7KOO contains 70 α-helices and 120 β-strands across 10 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: 12 helices, 16 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
α-helix	81-83	3
β-strand	89-91	3	2
β-strand	94	1	1
β-strand	102	1	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	160-162	3
β-strand	163	1	1
β-strand	173-177	5	2
β-strand	180-185	6	2
β-strand	186-187	2	3
β-strand	194-205	12	2
α-helix	208-213	6
α-helix	216-226	11
α-helix	227-230	4
α-helix	238-259	22
α-helix	269-295	27
α-helix	306-320	15
α-helix	409-464	56
α-helix	470-477	8

Chains F, G, H, I and J: 2 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	16
β-strand	5	1	17
β-strand	12	1	17
α-helix	14	1
β-strand	15	1	16
α-helix	16-17	2
β-strand	22-27	6	18
β-strand	39-40	2	3
β-strand	41-45	5	18
β-strand	56-57	2	18

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	562	Homo sapiens, Escherichia coli	P0ABE7 (AlphaFold model), P36544 (AlphaFold model)
Alpha-bungarotoxin isoform V31	F, G, H, I, J	protein	71	Bungarus multicinctus	P60616 (AlphaFold model)

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

>7KOO_1 Neuronal acetylcholine receptor subunit alpha-7,Soluble cytochrome b562 fusion (chains A, B, C, D, E)
EFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWT
DHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPP
GIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPG
KRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKIS
LGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPD
GGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMAGAMADLEDNWE
TLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDIL
VGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLCGRMACSPTHDEHLLHGGQPPE
GDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILM
SAPNFVEAVSKDFAWSHPQFEK

Sequence of entity 2 (F, G, H, I, J), FASTA

>7KOO_2 Alpha-bungarotoxin isoform V31 (chains F, G, H, I, J)
IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCC
STDKCNPHPKQ

Ligands and cofactors

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

Primary citation

Structure and gating mechanism of the alpha 7 nicotinic acetylcholine receptor. Noviello, C.M., Gharpure, A., Mukhtasimova, N. et al. Cell (2021) 184:2121. DOI 10.1016/j.cell.2021.02.049 · 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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