4AQ5: Acetylcholine receptor subunit alpha

Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class). Determined by electron microscopy at 6.2 Å resolution. Released 1 Aug 2012.

Method: Electron microscopy
Resolution: 6.2 Å
Organism: TORPEDO MARMORATA
Chains: 5
Atoms: 14,924
Mol. weight: 278.07 kDa
Released: 1 Aug 2012

Explore 4AQ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AQ5 contains 47 α-helices and 77 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: 12 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	29-44	16	1
β-strand	49-60	12	1
β-strand	66	1	2
α-helix	72-75	4
β-strand	78-81	4	1
α-helix	82-84	3
β-strand	90-92	3	3
β-strand	107-110	4	1
β-strand	113	1	2
β-strand	116-118	3	1
β-strand	121-127	7	1
α-helix	132-134	3
β-strand	140-148	9	3
β-strand	156-159	4	1
α-helix	167-169	3
β-strand	177-187	11	3
β-strand	199-208	10	3
α-helix	213-238	26
α-helix	240-242	3
α-helix	245-270	26
α-helix	275-277	3
α-helix	278-300	23
α-helix	376-398	23
α-helix	406-435	30

Chain B: 10 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	4-14	11
β-strand	30-34	5	4
β-strand	37-44	8	5
β-strand	49-55	7	5
β-strand	57-61	5	4
α-helix	69-72	4
β-strand	78-80	3	4
β-strand	91-92	2	6
β-strand	100-101	2	5
β-strand	108-110	3	4
β-strand	115-118	4	4
β-strand	121-126	6	5
β-strand	143-147	5	6
β-strand	153	1	7
β-strand	157-159	3	4
α-helix	177-179	3
β-strand	187	1	8
β-strand	194-195	2	6
β-strand	204	1	7
β-strand	207-210	4	6
β-strand	214	1	8
α-helix	225-240	16
α-helix	246-249	4
α-helix	251-269	19
α-helix	282-306	25
α-helix	405-429	25
α-helix	433-446	14
α-helix	449-461	13

Chain C: 8 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	33-46	14	9
β-strand	51-63	13	9
α-helix	71-75	5
β-strand	80-82	3	9
α-helix	84-86	3
β-strand	92-94	3	10
β-strand	103	1	9
β-strand	110-112	3	9
β-strand	117-120	4	9
β-strand	123-128	6	9
β-strand	143-150	8	10
β-strand	160-161	2	9
β-strand	190-194	5	10
β-strand	197-201	5	10
β-strand	213-223	11	10
α-helix	228-246	19
α-helix	249-253	5
α-helix	257-281	25
α-helix	289-313	25
α-helix	428-445	18
α-helix	453-476	24

Chain D: 9 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	30-32	3	11
β-strand	37-44	8	12
β-strand	49-55	7	12
β-strand	58-60	3	11
α-helix	63-65	3
α-helix	72-75	4
β-strand	78-81	4	13
β-strand	90-92	3	14
β-strand	101	1	12
β-strand	107-110	4	13
β-strand	116-118	3	11
β-strand	121-127	7	12
β-strand	140-148	9	14
β-strand	157-159	3	11
β-strand	177-187	11	14
β-strand	199-208	10	14
α-helix	213-239	27
α-helix	243-268	26
α-helix	275-277	3
α-helix	278-300	23
α-helix	375-398	24
α-helix	406-435	30

Chain E: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
β-strand	30-39	10	15
β-strand	43	1	16
β-strand	48	1	16
β-strand	49-50	2	17
β-strand	51-60	10	15
β-strand	89-90	2	18
β-strand	100	1	19
β-strand	109	1	15
β-strand	114-117	4	15
β-strand	120-121	2	15
β-strand	122	1	19
β-strand	124-125	2	17
α-helix	138-141	4
β-strand	143-145	3	20
β-strand	146-147	2	18
β-strand	157-158	2	15
α-helix	173-175	3
β-strand	183-187	5	21
β-strand	191-193	3	20
β-strand	207-210	4	20
β-strand	213-216	4	21
α-helix	222-245	24
α-helix	250-278	29
α-helix	283-306	24
α-helix	415-440	26
α-helix	444-473	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acetylcholine receptor subunit alpha	A, D	protein	461	TORPEDO MARMORATA	P02711 (AlphaFold model)
Acetylcholine receptor beta subunit	B	protein	493	TORPEDO MARMORATA	Q6S3I0 (AlphaFold model)
Acetylcholine receptor delta subunit	C	protein	522	TORPEDO MARMORATA	Q6S3H8 (AlphaFold model)
Acetylcholine receptor gamma subunit	E	protein	488	TORPEDO MARMORATA	Q6S3H9 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>4AQ5_1 ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA (chains A, D)
MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQ
LIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNA
DGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKV
SISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVV
NVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGK
YMLFTMIFVISSIIVTVVVINTHHRSPSTHTMPQWVRKIFINTIPNVMFFSTMKRASKEK
QENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAA
EEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Sequence of entity 2 (B), FASTA

>4AQ5_2 ACETYLCHOLINE RECEPTOR BETA SUBUNIT (chains B)
MEDVRRMALGLVVMMALALSGVGASVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLT
LTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNN
DGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEV
ILQHALDAKGEREVKEIMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRK
PLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLS
VPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPV
TTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVT
LPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFL
DASHNVPPDNPFA

Sequence of entity 3 (C), FASTA

>4AQ5_3 ACETYLCHOLINE RECEPTOR DELTA SUBUNIT (chains C)
MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTL
SNLISLKETDETLTTNVWMDHAWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNND
GQYNVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEIS
MDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYGDKFPNGTNYQDVTFYL
IIRRKPLFYVINFITPCVLISFLAALAFYLPAESGEKMSTAICVLLAQAVFLLLTSQRLP
ETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILH
MSRVDEIEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPR
IGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMF
IITPVMVLGTIFIFVMGNFNRPPAKPFEGDPFDYSSDHPRCA

Sequence of entity 4 (E), FASTA

>4AQ5_4 ACETYLCHOLINE RECEPTOR GAMMA SUBUNIT (chains E)
NEEGRLIEKLLGDYDKRIKPAKTLDHVIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWN
DYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPP
AIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGEVVEWIHIDPEDFTEN
GEWTIRHRPAKKNYNWQLTKDDIDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVY
FLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSLVIVTNC
VIVLNVSLRTPNTHSLSEKIKHLFLEFLPKYLGMHLEPSEETPEKPQPRRRSSFGIMIKA
EEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACN
FIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSLGTLAIFLTGHLNQVPEFPFP
GDPRKYVP

Primary citation

Gating Movement of Acetylcholine Receptor Caught by Plunge-Freezing. Unwin, N., Fujiyoshi, Y. J Mol Biol (2012) 422:617. DOI 10.1016/J.JMB.2012.07.010 · PubMed

Other PDB entries of the same protein (UniProt P02711 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1OED 4.0 Å, Structure of acetylcholine receptor pore from electron images
2BG9 4.0 Å, Refined structure of the nicotinic acetylcholine receptor at 4A resolution.
4AQ9 6.2 Å, Gating movement in acetylcholine receptor analysed by time- resolved electron…
4BON 40.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class B
4BOI 41.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class A
4BOO 42.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class C
4BOR 42.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes class D
4BOT 42.0 Å, The structure and super-organization of acetylcholine receptor- rapsyn complexes class E
4BOG 50.0 Å, The structure and super-organization of acetylcholine receptor-rapsyn complexes
1L4W NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202)…
1LJZ NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202)…

Browse structure collections

About this viewer

MolViewer shows 4AQ5 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.