SAXSdb — 9iqr

▼

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

Muscarinic toxin 3

Dendroaspis angusticeps

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–65	Not recorded	Alpha-2A adrenergic receptor,Soluble cytochrome b562 × 1 （P08913）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen NITROGEN	Resolution 3.40 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 9IQR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
9IQS Cryo-EM structure of MT3-Muscarinic acetylcholine receptor 4 Deposited 2024-07-13	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–65（65 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.60 Å
9IQV Cryo-EM structure of MT3-alpha1AAR Deposited 2024-07-13	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–65（65 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.30 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	3SIM3_DENAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–65； UniProt 1–65

Alpha-2A adrenergic receptor,Soluble cytochrome b562

Homo sapiens

UniProt P08913

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 38–241 Chain B； UniProt 379–456	Not recorded	Muscarinic toxin 3 × 1 （P81031）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen NITROGEN	Resolution 3.40 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 9IQR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1HLL NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTOR Deposited 2000-12-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 118–149（32 aa） Fragment：SECOND INTRACELLULAR LOOP T3-I2 (RESIDUES 118-149)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NaCl NMR sample composition 0.9 mM T3-I2 natural abundance; 460 mM D38-dodecylphosphocholine, 50 mM NaCl, 10 mM NaH2PO4, pH 4.5 \| 90% H2O/10% D2O NMR sample composition 0.9 mM T3-I2 natural abundance; 460 mM D38 dodecylphosphocholine, 50 mM NaCl, 10 mM NaH2PO4, pH 4.5 \| 100% D2O	Resolution not provided
1HO9 BEST 20 NMR CONFORMERS OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA 2A ADRENERGIC RECEPTOR Deposited 2000-12-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 118–149（32 aa） Fragment：SECOND INTRACELLULAR LOOP (RESIDUES 118-149)	Mutation：D130I	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NACL NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NMR sample composition 0.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 90% H2O/10% D2O NMR sample composition 0.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 100% D20	Resolution not provided
1HOD NMR STRUCTURE OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA 2A ADRENERGIC RECEPTOR Deposited 2000-12-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 118–149（32 aa） Fragment：SECOND INTRACELLULAR LOOP (RESIDUES 118-149)	Mutation：D130I	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NACL NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NMR sample composition 0.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 90% H2O/10% D2O NMR sample composition 0.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 100 % D20	Resolution not provided
1HOF NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A ADRENERGIC RECEPTOR Deposited 2000-12-10	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 118–149（32 aa） Fragment：SECOND INTRACELLULAR LOOP (RESIDUES 118-149)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NACL NMR measurement conditions pH 4.5；303 K；Ionic strength (raw mmCIF value) 50 mM NMR sample composition 0.9 MM T3-I2 PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 90% H2O/10% D2O NMR sample composition 0.9 MM T3-I2 PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5 \| 100% D2O	Resolution not provided
6K42 cryo-EM structure of alpha2BAR-Gi1 complex Deposited 2019-05-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–27（27 aa）	Not recorded	CZX 4-[(1~{S})-1-(2,3-dimethylphenyl)ethyl]-1~{H}-imidazole × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
7EJ0 Structure of the alpha2A-adrenergic receptor GoA signaling complex Deposited 2021-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	E5E Noradrenaline × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7EJ8 Structure of the alpha2A-adrenergic receptor GoA signaling complex bound to brimonidine Deposited 2021-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	J59 Brimonidine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
7EJA Structure of the alpha2A-adrenergic receptor GoA signaling complex bound to dexmedetomidine Deposited 2021-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	CZX 4-[(1~{S})-1-(2,3-dimethylphenyl)ethyl]-1~{H}-imidazole × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7EJK Structure of the alpha2A-adrenergic receptor GoA signaling complex bound to oxymetazoline Deposited 2021-04-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	J5C Oxymetazoline × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
7W6P Cryo-EM structure of the alpha2A adrenergic receptor GoA signaling complex bound to a G protein biased agonist Deposited 2021-12-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	W96 N-pyridin-4-ylisoquinolin-4-amine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.47 Å
7W7E Cryo-EM structure of the alpha2A adrenergic receptor GoA signaling complex bound to a biased agonist Deposited 2021-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 1–465（465 aa）	Not recorded	W58 5-(3-bicyclo[4.2.0]octa-1,3,5-trienyl)-1,2,3,6-tetrahydropyridine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9CBL Cryo-EM structure of epinephrine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein Deposited 2024-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 35–242（208 aa） Chain R 380–460（81 aa）	Not recorded	ALE L-EPINEPHRINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9CBM Cryo-EM structure of dexmedetomidine-bound alpha-2A-adrenergic receptor in complex with heterotrimeric Gi-protein Deposited 2024-06-19	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 35–242（208 aa） Chain R 380–460（81 aa）	Not recorded	CZX 4-[(1~{S})-1-(2,3-dimethylphenyl)ethyl]-1~{H}-imidazole × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9PLN Locally-refined structure of alpha2a adrenergic receptor in complex with Go heterotrimer, scFv16, and N-(5-methylnaphthalen-1-yl)pyridin-4-amine (compound 4905) Deposited 2025-07-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain R 2–465（464 aa）	Not recorded	A1CIU N-(5-methylnaphthalen-1-yl)pyridin-4-amine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHS was solubilized in LMNG and GDN prior to diluting into buffers. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9PLO Structure of alpha2a adrenergic receptor in complex with Go heterotrimer, scFv16, and N-(5-methylnaphthalen-1-yl)pyridin-4-amine (compound 4905) Deposited 2025-07-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–465（464 aa）	Not recorded	A1CIU N-(5-methylnaphthalen-1-yl)pyridin-4-amine × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；CHS was solubilized in LMNG and GDN prior to diluting into buffers. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
9PQD Locally-refined structure of alpha2a adrenergic receptor in complex with Go heterotrimer, scFv16, and compound Z7149 Deposited 2025-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain R 2–465（464 aa）	Not recorded	A1CIZ (6M)-1-methyl-6-(1,2,5,6-tetrahydropyridin-3-yl)-1H-indole × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；Buffer was supplemented with 0.01 mM compound Z7149 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ADA2A_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–204； UniProt 38–241 Author chain B； PDBConstruct 306–383； UniProt 379–456

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	9iqr
Deposition date deposition_date	2024-07-13
Structure title title	Cryo-EM structure of MT3-alpha2AAR
Keywords keywords	complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	24.83 Å
Radius of gyration Rg (electron density) rg_electron	23.68 Å
Forward intensity I(0) i0	20299500.00
Molecular weight molecular_weight	37219.0 kDa
Excluded volume excluded_volume	47884 Å³
Envelope volume envelope_volume	58636 Å³
Hydration-shell volume shell_volume	22007 Å³
Envelope diameter envelope_diameter	87.7 Å
Shell Rg shell_rg	29.35 Å
Envelope Rg envelope_rg	24.19 Å
Shape Rg shape_rg	23.60 Å
Total Rg total_rg	24.76 Å
Total atoms total_atoms	2622
Residues n_residues	325
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

▼

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

Maximum dimension Dmax dmax	84.4 Å
Rg (real space) rg_real	25.08 Å
Rg uncertainty (real space) rg_real_error	0.66 Å
I(0) (real space) i0_real	2.0300e+07
I(0) uncertainty (real space) i0_real_error	2.8860e+05
Rg (reciprocal space) rg_reciprocal	25.02 Å
I(0) (reciprocal space) i0_reciprocal	20300000.0000
Solution quality estimate total_estimate	0.8456
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	24.1 Å
Skewness Skewness skewness	0.544
Kurtosis Kurtosis kurtosis	-0.259
Angular range angular_range	— – 0.3200 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2601000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.768; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.755; Smooth: 0.930

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Muscarinic toxin 3
Molecular weight formula_weight	7396.5 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	2622

LTCVTKNTIFGITTENCPAGQNLCFKRWHYVIPRYTEITRGCAATCPIPENYDSIHCCKTDKCNE

来源 Source

来源生物 organism	Dendroaspis angusticeps
通用名 common_name	eastern green mamba
NCBI Class编号 ncbi_taxonomy_id	8618
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Alpha-2A adrenergic receptor,Soluble cytochrome b562
Molecular weight formula_weight	48895.1 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

ARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRAADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKASGSGSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLAGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILKIAALKEKIAALKEKIAALKEAEEKRASRLEEELRRRLTEGSHHHHHHHH

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	Homo sapiens

▶

8. Citations (1)

▶

Resolution resolution	3.40 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	2264441

fit	/app/data/saxs_computation/iq/9iqr/9iqr.fit
pddf	/app/data/pr_computation/iq/9iqr/9iqr.pr.out
profile	/app/data/saxs_computation/iq/9iqr/9iqr.dat

Cryo-EM structure of MT3-alpha2AAR

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

Muscarinic toxin 3

State in the Current Structure

Other States of the Same Protein in the Database

Alpha-2A adrenergic receptor,Soluble cytochrome b562

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)