8qqm

nicotinic acetylcholine receptor in intact synaptic membrane

Method: ELECTRON MICROSCOPY Dmax: 97.7 Å Quality: REASONABLE

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

Acetylcholine receptor subunit alpha

OrganismNot specified

UniProt P02710

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 25–461 Chain D; UniProt 25–461 Not recorded Acetylcholine receptor subunit delta × 1 (P02718) Acetylcholine receptor subunit beta × 1 (P02712) Acetylcholine receptor subunit gamma × 1 (P02714) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACHA_TETCF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–437; UniProt 25–461 Author chain D; PDBConstruct 1–437; UniProt 25–461

Acetylcholine receptor subunit delta

OrganismNot specified

UniProt P02718

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 22–522 Not recorded Acetylcholine receptor subunit alpha × 2 (P02710) Acetylcholine receptor subunit beta × 1 (P02712) Acetylcholine receptor subunit gamma × 1 (P02714) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACHD_TETCF
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–501; UniProt 22–522

Acetylcholine receptor subunit beta

OrganismNot specified

UniProt P02712

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 25–493 Not recorded Acetylcholine receptor subunit alpha × 2 (P02710) Acetylcholine receptor subunit delta × 1 (P02718) Acetylcholine receptor subunit gamma × 1 (P02714) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACHB_TETCF
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–469; UniProt 25–493

Acetylcholine receptor subunit gamma

OrganismNot specified

UniProt P02714

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 18–506 Not recorded Acetylcholine receptor subunit alpha × 2 (P02710) Acetylcholine receptor subunit delta × 1 (P02718) Acetylcholine receptor subunit beta × 1 (P02712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACHG_TETCF
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–489; UniProt 18–506

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8qqm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qqm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qqm
Deposition date deposition_date2023-10-05
最后修订 last_revision2024-05-08
Structure title titlenicotinic acetylcholine receptor in intact synaptic membrane
Keywords keywordsIon channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.20
Radius of gyration Rg (electron density) rg_electron30.46
Forward intensity I(0) i0128383000.00
Molecular weight molecular_weight101120.0 kDa
Excluded volume excluded_volume131610 ų
Envelope volume envelope_volume172660 ų
Hydration-shell volume shell_volume46507 ų
Envelope diameter envelope_diameter104.6
Shell Rg shell_rg38.42
Envelope Rg envelope_rg30.23
Shape Rg shape_rg30.48
Total Rg total_rg31.22
Total atoms total_atoms7118
Residues n_residues901
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax97.7
Rg (real space) rg_real31.09
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.2840e+08
I(0) uncertainty (real space) i0_real_error2.1860e+06
Rg (reciprocal space) rg_reciprocal31.14
I(0) (reciprocal space) i0_reciprocal128400000.0000
Solution quality estimate total_estimate0.6421
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.2
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.130
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24110000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 1.000; Sysdev: 0.011; Positv: 1.000; Valcen: 0.990; Smooth: 0.769

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)