1oed

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

Method: ELECTRON MICROSCOPY

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Acetylcholine receptor subunit alpha

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 5	Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor delta subunit × 1 （Q6S3H8） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ACHA_TORMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–227； UniProt 235–461 Author chain D； PDBConstruct 1–227； UniProt 235–461

Acetylcholine receptor beta subunit

OrganismNot specified

UniProt Q6S3I0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 5	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor delta subunit × 1 （Q6S3H8） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6S3I0_TORMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–250； UniProt 241–490

Acetylcholine receptor delta subunit

OrganismNot specified

UniProt Q6S3H8

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 5	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6S3H8_TORMA
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–260； UniProt 246–505

Acetylcholine receptor gamma subunit

OrganismNot specified

UniProt Q6S3H9

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 5	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor delta subunit × 1 （Q6S3H8）	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6S3H9_TORMA
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–260； UniProt 235–494

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1oed
Deposition date deposition_date	2003-03-24
Structure title title	STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES
Keywords keywords	ION CHANNEL/RECEPTOR, ION CHANNEL, TUBULAR CRYSTAL, ACETYLCHOLINE RECEPTOR, TRANSMEMBRANE, ION CHANNEL-RECEPTOR complex; ION CHANNEL/RECEPTOR
Experimental Method method	ELECTRON MICROSCOPY

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1oed__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1oed__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1oed__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	27.31 Å
Rg (electron density)	25.91 Å
Total Rg	26.91 Å
Atom count	4926
Residues	636
Excluded volume	92317 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1oed__assembly_1__model_1`	pentameric （5）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Acetylcholine receptor subunit alpha
Molecular weight formula_weight	25389.0 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	4926

PLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Entity 2 Entity 2 polymer

Description description	Acetylcholine receptor beta subunit
Molecular weight formula_weight	28387.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

PLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDN

Entity 3 Entity 3 polymer

Description description	Acetylcholine receptor delta subunit
Molecular weight formula_weight	29371.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

PLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAK

Entity 4 Entity 4 polymer

Description description	Acetylcholine receptor gamma subunit
Molecular weight formula_weight	29321.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

PLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEF

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d1oeda_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedc_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedd_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oede_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

CATH v4.4 (5 domains)

Domain ID domain_id	1oedA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	1oedB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	1oedC00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	1oedD00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	1oedE00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	4.00 Å
Resolution测定Method resolution_method	—
颗粒数 num_particles	—

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

1. Protein Identity and Related Structures Protein Identity & Related Structures

Acetylcholine receptor subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor delta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor gamma subunit

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1oed__assembly_1__model_1

1oed__assembly_1__model_1 | I(q)

1oed__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (4)

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

1. Protein Identity and Related Structures Protein Identity & Related Structures

Acetylcholine receptor subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Acetylcholine receptor beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Acetylcholine receptor delta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Acetylcholine receptor gamma subunit

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

1oed__assembly_1__model_1

1oed__assembly_1__model_1 | I(q)

1oed__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

7. Citations (4)