SAXSdb — 8ea0

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

Muscarinic acetylcholine receptor M3

Homo sapiens

UniProt P20309

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 46–283 Chain A； UniProt 464–590	Not recorded	IXO 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE-PROPANE	Resolution 2.56 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.

Other PDB	Difference from Current Entry 8EA0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2CSA Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal Deposited 2005-05-21	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 271–289（19 aa） Fragment：THIRD INTRACELLULAR LOOP (Residues:271-289)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.4；285 K；Pressure ambient NMR measurement conditions pH 6.4；278 K；Pressure ambient NMR measurement conditions pH 6.4；288 K；Pressure ambient NMR measurement conditions pH 6.4；298 K；Pressure ambient NMR measurement conditions pH 6.4；308 K；Pressure ambient NMR measurement conditions pH 6.4；318 K；Pressure ambient NMR sample composition 1-2mM M3 peptide, unlabeled, 50mM sodium phosphate buffer, 1mM EDTA, 1mM NaN3, 90% H2O, 10% D20 \| 90% H2O, 10% D20 NMR sample composition 1-2mM M3 peptide, unlabeled, 50mM sodium phosphate buffer, 1mM EDTA, 1mM NaN3, 99.9 % D20, 0.1% H20 \| 99.9 % D20, 0.1% H20	Resolution not provided
8E9W CryoEM structure of miniGq-coupled hM3Dq in complex with DCZ Deposited 2022-08-27	Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 46–283（238 aa） Chain A 464–590（127 aa）	Mutation：Y149C, A239G Mutation：Y149C, A239G	WEC 11-(4-methylpiperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.69 Å
8E9Y CryoEM structure of miniGq-coupled hM3Dq in complex with CNO Deposited 2022-08-27	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 46–283（238 aa） Chain A 464–590（127 aa）	Not recorded	WE9 8-chloro-11-(4-methyl-4-oxo-4lambda~5~-piperazin-1-yl)-5H-dibenzo[b,e][1,4]diazepine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.79 Å
8E9Z CryoEM structure of miniGq-coupled hM3R in complex with Iperoxo Deposited 2022-08-27	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 46–283（238 aa） Chain A 464–590（127 aa）	Not recorded	IXO 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium × 1 Y01 CHOLESTEROL HEMISUCCINATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 2.69 Å

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACM3_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–238； UniProt 46–283 Author chain A； PDBConstruct 239–365； UniProt 464–590

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	8ea0
Deposition date deposition_date	2022-08-27
Structure title title	CryoEM structure of miniGq-coupled hM3R in complex with iperoxo (local refinement)
Keywords keywords	GPCR, IXO, active state, MEMBRANE PROTEIN, hM3R, Iperoxo; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	21.59 Å
Radius of gyration Rg (electron density) rg_electron	20.48 Å
Forward intensity I(0) i0	14747800.00
Molecular weight molecular_weight	32416.0 kDa
Excluded volume excluded_volume	42112 Å³
Envelope volume envelope_volume	49365 Å³
Hydration-shell volume shell_volume	20416 Å³
Envelope diameter envelope_diameter	71.6 Å
Shell Rg shell_rg	26.94 Å
Envelope Rg envelope_rg	21.03 Å
Shape Rg shape_rg	20.46 Å
Total Rg total_rg	21.59 Å
Total atoms total_atoms	2286
Residues n_residues	285
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	71.7 Å
Rg (real space) rg_real	21.61 Å
Rg uncertainty (real space) rg_real_error	0.47 Å
I(0) (real space) i0_real	1.4750e+07
I(0) uncertainty (real space) i0_real_error	1.9970e+05
Rg (reciprocal space) rg_reciprocal	21.61 Å
I(0) (reciprocal space) i0_reciprocal	14750000.0000
Solution quality estimate total_estimate	0.8837
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.2 Å
Skewness Skewness skewness	0.352
Kurtosis Kurtosis kurtosis	-0.376
Angular range angular_range	— – 0.3700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2107000.0000
Real-space data points n_real_points	69
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.987

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Muscarinic acetylcholine receptor M3
Molecular weight formula_weight	62966.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2286

AGNFSSPDGTTDDPLGGHTVWQVVFIAFLTGILALVTIIGNILVIVSFKVNKQLKTVNNYFLLSLACADLIIGVISMNLFTTYIIMNRWALGNLACDLWLAIDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTTKRAGVMIGLAWVISFVLWAPAILFWQYFVGKRTVPPGECFIQFLSEPTITFGTAIAAFYMPVTIMTILYWRIYKETEKRTKELAGLQASGTEAETENFVHPAKRFALKTRSQITKRKRMSLVKEKKAAQTLSAILLAFIITWTPYNIMVLVNTFCDSCIPKTFWNLGYWLCYINSTVNPVCYALCNKTFRTTFKMLLLCQCDKKKRRKQQYQQRQSVIFHKRAPEQALGGSGGGGSGGSSSGGGGSGGGGSGGSSSGGVFTLEDFVGDWEQTAAYNLDQVLEQGGVSSLLQNLAVSVTPIQRIVRSGENALKIDIHVIIPYEGLSADQMAQIEEVFKVVYPVDDHHFKVILPYGTLVIDGVTPNMLNYFGRPYEGIAVFDGKKITVTGTLWNGNKIIDERLITPDGSMLFRVTINSGGSGGHHHHHHHHHH

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 non-polymer

Description description	4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium
Molecular weight formula_weight	197.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	CHOLESTEROL HEMISUCCINATE
Molecular weight formula_weight	486.7 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	8ea0A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily	10 — Rhodopsin 7-helix transmembrane proteins

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8. Citations (1)

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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	—

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

Resolution resolution	2.56 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	591814

fit	/app/data/saxs_computation/ea/8ea0/8ea0.fit
pddf	/app/data/pr_computation/ea/8ea0/8ea0.pr.out
profile	/app/data/saxs_computation/ea/8ea0/8ea0.dat

CryoEM structure of miniGq-coupled hM3R in complex with iperoxo (local refinement)

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

Muscarinic acetylcholine receptor M3

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D