4AQ9: Acetylcholine receptor subunit alpha

Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open 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 4AQ9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4AQ9 contains 52 α-helices and 73 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: 11 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	29-44	16	1
β-strand	49-60	12	1
α-helix	72-75	4
β-strand	79-81	3	1
α-helix	82-84	3
β-strand	90-92	3	2
β-strand	107-110	4	1
β-strand	116-118	3	1
β-strand	121-127	7	1
α-helix	132-134	3
β-strand	141-148	8	2
β-strand	156-159	4	1
α-helix	167-169	3
β-strand	180-187	8	2
β-strand	199-206	8	2
α-helix	213-237	25
α-helix	240-242	3
α-helix	246-269	24
α-helix	275-299	25
α-helix	376-398	23
α-helix	406-435	30

Chain B: 9 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	4-14	11
β-strand	30-44	15	3
β-strand	49-61	13	3
α-helix	69-73	5
β-strand	78-80	3	3
β-strand	91-92	2	4
β-strand	100-101	2	3
β-strand	108-110	3	3
β-strand	115-118	4	3
β-strand	121-126	6	3
β-strand	143-147	5	4
β-strand	153	1	5
β-strand	157-159	3	3
α-helix	177-179	3
β-strand	187	1	6
β-strand	194-195	2	4
β-strand	204	1	5
β-strand	207-210	4	4
β-strand	214	1	6
α-helix	225-240	16
α-helix	251-273	23
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
α-helix	4-11	8
β-strand	33-46	14	7
β-strand	51-63	13	7
β-strand	80-82	3	7
α-helix	84-86	3
β-strand	92-94	3	8
β-strand	103	1	7
β-strand	110-112	3	7
β-strand	117-120	4	7
β-strand	123-128	6	7
β-strand	143-150	8	8
β-strand	160-161	2	7
β-strand	190-194	5	8
β-strand	197-202	6	8
β-strand	211-223	13	8
α-helix	228-253	26
α-helix	257-283	27
α-helix	289-314	26
α-helix	422-442	21
α-helix	445-448	4
α-helix	453-476	24

Chain D: 13 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
β-strand	30-44	15	9
β-strand	49-60	12	9
α-helix	63-65	3
α-helix	72-75	4
β-strand	79-81	3	10
α-helix	82-84	3
β-strand	92	1	11
α-helix	99-100	2
β-strand	101	1	9
β-strand	107-109	3	10
β-strand	116-118	3	9
β-strand	121-127	7	9
β-strand	141-146	6	11
β-strand	157-159	3	9
β-strand	177-187	11	11
β-strand	199-208	10	11
α-helix	213-239	27
α-helix	240-242	3
α-helix	243-258	16
α-helix	260-268	9
α-helix	275-277	3
α-helix	278-300	23
α-helix	375-398	24
α-helix	405-435	31

Chain E: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
β-strand	28-39	12	12
β-strand	43	1	13
β-strand	48	1	13
β-strand	49-50	2	14
β-strand	51-60	10	12
β-strand	77-78	2	12
β-strand	89-90	2	15
β-strand	100	1	16
β-strand	108-109	2	12
β-strand	114-117	4	12
β-strand	120-121	2	12
β-strand	122	1	16
β-strand	124-125	2	14
α-helix	138-139	2
β-strand	140	1	17
β-strand	143-145	3	18
β-strand	146-147	2	15
β-strand	155-158	4	12
α-helix	173-175	3
β-strand	183-187	5	17
β-strand	192-193	2	18
β-strand	207-210	4	18
β-strand	213-216	4	17
α-helix	223-239	17
α-helix	242-245	4
α-helix	251-278	28
α-helix	283-306	24
α-helix	415-440	26
α-helix	444-461	18
α-helix	462-466	5
α-helix	467-473	7

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

>4AQ9_1 ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA (chains A, D)
MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQ
LIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNA
DGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKV
SISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVV
NVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGK
YMLFTMIFVISSIIVTVVVINTHHRSPSTHTMPQWVRKIFINTIPNVMFFSTMKRASKEK
QENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAA
EEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Sequence of entity 2 (B), FASTA

>4AQ9_2 ACETYLCHOLINE RECEPTOR BETA SUBUNIT (chains B)
MEDVRRMALGLVVMMALALSGVGASVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLT
LTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNN
DGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEV
ILQHALDAKGEREVKEIMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRK
PLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLS
VPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPV
TTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVT
LPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFL
DASHNVPPDNPFA

Sequence of entity 3 (C), FASTA

>4AQ9_3 ACETYLCHOLINE RECEPTOR DELTA SUBUNIT (chains C)
MGNIHFVYLLISCLYYSGCSGVNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTL
SNLISLKETDETLTTNVWMDHAWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNND
GQYNVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEIS
MDLMTDTIDGKDYPIEWIIIDPEAFTENGEWEIIHKPAKKNIYGDKFPNGTNYQDVTFYL
IIRRKPLFYVINFITPCVLISFLAALAFYLPAESGEKMSTAICVLLAQAVFLLLTSQRLP
ETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILH
MSRVDEIEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPR
IGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMF
IITPVMVLGTIFIFVMGNFNRPPAKPFEGDPFDYSSDHPRCA

Sequence of entity 4 (E), FASTA

>4AQ9_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.
4AQ5 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)…

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