4bog

The structure and super-organization of acetylcholine receptor-rapsyn complexes

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

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 30 Acetylcholine receptor delta subunit × 6 (Q6S3H8) Acetylcholine receptor subunit alpha × 12 (P02711) Acetylcholine receptor gamma subunit × 6 (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 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–493; UniProt 1–493 Author chain B; PDBConstruct 1–493; UniProt 1–493 Author chain G; PDBConstruct 1–493; UniProt 1–493 Author chain L; PDBConstruct 1–493; UniProt 1–493 Author chain Q; PDBConstruct 1–493; UniProt 1–493 Author chain V; PDBConstruct 1–493; UniProt 1–493

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 30 Acetylcholine receptor beta subunit × 6 (Q6S3I0) Acetylcholine receptor subunit alpha × 12 (P02711) Acetylcholine receptor gamma subunit × 6 (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 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–522; UniProt 1–522 Author chain C; PDBConstruct 1–522; UniProt 1–522 Author chain H; PDBConstruct 1–522; UniProt 1–522 Author chain M; PDBConstruct 1–522; UniProt 1–522 Author chain R; PDBConstruct 1–522; UniProt 1–522 Author chain W; PDBConstruct 1–522; UniProt 1–522

Acetylcholine receptor subunit alpha

OrganismNot specified

UniProt P02711

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 30 Acetylcholine receptor beta subunit × 6 (Q6S3I0) Acetylcholine receptor delta subunit × 6 (Q6S3H8) Acetylcholine receptor gamma subunit × 6 (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 3
Chains and sequence ranges Author chain 2; PDBConstruct 1–461; UniProt 1–461 Author chain A; PDBConstruct 1–461; UniProt 1–461 Author chain D; PDBConstruct 1–461; UniProt 1–461 Author chain F; PDBConstruct 1–461; UniProt 1–461 Author chain I; PDBConstruct 1–461; UniProt 1–461 Author chain K; PDBConstruct 1–461; UniProt 1–461 Author chain N; PDBConstruct 1–461; UniProt 1–461 Author chain P; PDBConstruct 1–461; UniProt 1–461 Author chain S; PDBConstruct 1–461; UniProt 1–461 Author chain U; PDBConstruct 1–461; UniProt 1–461 Author chain X; PDBConstruct 1–461; UniProt 1–461 Author chain Z; PDBConstruct 1–461; UniProt 1–461

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 30 Acetylcholine receptor beta subunit × 6 (Q6S3I0) Acetylcholine receptor delta subunit × 6 (Q6S3H8) Acetylcholine receptor subunit alpha × 12 (P02711) 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 3; PDBConstruct 1–505; UniProt 1–505 Author chain E; PDBConstruct 1–505; UniProt 1–505 Author chain J; PDBConstruct 1–505; UniProt 1–505 Author chain O; PDBConstruct 1–505; UniProt 1–505 Author chain T; PDBConstruct 1–505; UniProt 1–505 Author chain Y; PDBConstruct 1–505; UniProt 1–505

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_id4bog
Deposition date deposition_date2013-05-20
Structure title titleThe structure and super-organization of acetylcholine receptor-rapsyn complexes
Keywords keywordsTRANSPORT PROTEIN, CLUSTERING, SYNAPSE, NEUROMUSCULAR JUNCTION, NICOTINIC, RAPSYN, 43K, ELECTRIC ORGAN; TRANSPORT PROTEIN
Experimental Method methodELECTRON 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.

4bog__assembly_1__model_1

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

Download this curve (.dat)

4bog__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

4bog__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)0.00 Å
Rg (electron density)100.40 Å
Total Rg100.20 Å
Atom count89544
Residues11106
Excluded volume1618800 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 4bog__assembly_1__model_1 30-meric (30) 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)

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7. Citations (1)