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2csa

Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal

Method: SOLUTION NMR Dmax: 40.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Muscarinic acetylcholine receptor M3

OrganismNot specified

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 271–289 Fragment：THIRD INTRACELLULAR LOOP (Residues:271-289) No other associated polymer 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

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 2CSA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8E9W CryoEM structure of miniGq-coupled hM3Dq in complex with DCZ Deposited 2022-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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 construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions 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
8EA0 CryoEM structure of miniGq-coupled hM3R in complex with iperoxo (local refinement) Deposited 2022-08-27 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 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 2.56 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 1–19； UniProt 271–289

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 2csa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2csa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2csa
Deposition date deposition_date2005-05-21
Structure title titleStructure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal
Keywords keywordsBASOLATERAL SORTING-SIGNAL BLSS BETA-TURN, Signaling Protein-MEMBRANE PROTEIN COMPLEX; Signaling Protein/MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier10.41 Å
Radius of gyration Rg (electron density) rg_electron9.50 Å
Forward intensity I(0) i08903800.00
Molecular weight molecular_weight19740.0 kDa
Excluded volume excluded_volume23247 ų
Envelope volume envelope_volume12260 ų
Hydration-shell volume shell_volume8900 ų
Envelope diameter envelope_diameter39.9 Å
Shell Rg shell_rg17.41 Å
Envelope Rg envelope_rg12.48 Å
Shape Rg shape_rg9.44 Å
Total Rg total_rg10.65 Å
Total atoms total_atoms2460
Residues n_residues190
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax40.1 Å
Rg (real space) rg_real10.49 Å
Rg uncertainty (real space) rg_real_error0.41 Å
I(0) (real space) i0_real8.9040e+06
I(0) uncertainty (real space) i0_real_error9.6640e+04
Rg (reciprocal space) rg_reciprocal10.49 Å
I(0) (reciprocal space) i0_reciprocal8904000.0000
Solution quality estimate total_estimate0.8012
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.7 Å
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis0.087
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30530.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.634; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.568; Smooth: 0.942
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)