SAXSdb — 2lm2

▼

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

Neuronal acetylcholine receptor subunit beta-2

Homo sapiens

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 231–330 Chain A； UniProt 458–486	Fragment：Helical transmembrane region, residues 234-330 and residues 458-484 Mutation：R231E, R232E, K233E, L292S, V294S, L296S, K299E, T327E	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4.65；318 K；Pressure ambient NMR sample composition：0.25 mM [U-100% 13C; U-100% 15N] protein, 5 mM sodium acetate, 1.5 % LDAO, 0.1 mM DSS, 5 % [U-100% 2H] D2O, 10 mM sodium chloride, 20 mM beta-mercaptoethanol, 95% H2O/5% D2O \| 95% H2O/5% D2O	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 2LM2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2K58 NMR structures of the first transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit Deposited 2008-06-25	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 231–265（35 aa） Fragment：unp residues 231-265	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；303 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 0.83 mM [U-100% 15N] nAChR TM1, 0.5 mM DSS, 125 mM DPC, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2K59 NMR structures of the second transmembrane domain of the neuronal acetylcholine receptor beta 2 subunit Deposited 2008-06-25	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 264–291（28 aa） Fragment：UNP residues 264-291	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；303 K；Ionic strength (raw mmCIF value) 0.25；Pressure ambient NMR sample composition 3-5 mM [U-100% 15N] nAChR TM2, 0.5 mM DSS, 450-750 mM DPC, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2KSR NMR structures of TM domain of the n-Acetylcholine receptor b2 subunit Deposited 2010-01-12	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 231–330（100 aa） Chain A 453–486（34 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.8；313 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.2 mM [U-100% 13C; U-100% 15N] TM123, 50% HFIP/50% H2O \| 50% HFIP/50% H2O NMR sample composition 0.2 mM [U-100% 13C; U-100% 15N] TM1234, 50% HFIP/ 50% H2O \| 50% HFIP/ 50% H2O	Resolution not provided
5KXI X-ray structure of the human Alpha4Beta2 nicotinic receptor Deposited 2016-07-20	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 B 26–355（330 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502 Chain B 446–502（57 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502 Chain C 26–355（330 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502 Chain C 446–502（57 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502 Chain E 26–355（330 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502 Chain E 446–502（57 aa） Fragment：UNP residues 26-355,446-502,UNP residues 26-353,446-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 2 NA SODIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287.15 K；0.05 M ADA pH 6.8, 12.5% PEG 1500 and 10% PEG 1000	Resolution 3.94 Å R-free 0.307
6CNJ Structure of the 2alpha3beta stiochiometry of the human Alpha4Beta2 nicotinic receptor Deposited 2018-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain B 26–353（328 aa） Chain B 446–502（57 aa） Chain C 26–353（328 aa） Chain C 446–502（57 aa） Chain E 26–353（328 aa） Chain E 446–502（57 aa）	Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. Mutation：Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit.	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 2 Y01 CHOLESTEROL HEMISUCCINATE × 10 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；4 second blot time	Resolution 3.70 Å
6CNK Structure of the 3alpha2beta stiochiometry of the human Alpha4Beta2 nicotinic receptor Deposited 2018-03-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain C 26–353（328 aa） Chain C 446–502（57 aa） Chain E 26–353（328 aa） Chain E 446–502（57 aa）	Mutation：;Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit.,Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit.,Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit.,Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit.,Glu-Arg linker was inserted in the MX-M4 junction between Gln420-Ser421 in the beta 2 subunit. ;	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 Y01 CHOLESTEROL HEMISUCCINATE × 10 NA SODIUM ION × 1 NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；4 second blot time	Resolution 3.90 Å
6UR8 CryoEM structure of human alpha4beta2 nicotinic acetylcholine receptor in complex with varenicline Deposited 2019-10-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 26–351（326 aa） Chain B 442–502（61 aa） Chain C 26–351（326 aa） Chain C 442–502（61 aa） Chain E 26–351（326 aa） Chain E 442–502（61 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 QMR VARENICLINE × 2 BMA beta-D-mannopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.71 Å
6USF CryoEM structure of human alpha4beta2 nicotinic acetylcholine receptor with varenicline in complex with anti-BRIL synthetic antibody BAK5 Deposited 2019-10-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 9 PDB declaration: nonameric	Chain B 26–351（326 aa） Chain B 442–502（61 aa） Chain C 26–351（326 aa） Chain C 442–502（61 aa） Chain E 26–351（326 aa） Chain E 442–502（61 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 QMR VARENICLINE × 2 BMA beta-D-mannopyranose × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.87 Å
8SSZ The 2alpha3beta stoichiometry of full-length human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain B 26–502（477 aa） Chain C 26–502（477 aa） Chain E 26–502（477 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ACH ACETYLCHOLINE × 2 CA CALCIUM ION × 2 NA SODIUM ION × 1 OCT N-OCTANE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.64 Å
8ST0 The 2alpha3beta stoichiometry of full-length human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain B 26–502（477 aa） Chain C 26–502（477 aa） Chain E 26–502（477 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ACH ACETYLCHOLINE × 2 OCT N-OCTANE × 1 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
8ST1 The 3alpha2beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain C 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain C 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain E 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain E 442–502（61 aa） Fragment：UNP residues 26-355,442-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ACH ACETYLCHOLINE × 3 CA CALCIUM ION × 4 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.41 Å
8ST2 The 3alpha2beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain C 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain C 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain E 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain E 442–502（61 aa） Fragment：UNP residues 26-355,442-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ACH ACETYLCHOLINE × 3 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
8ST3 The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain B 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain B 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain C 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain C 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain E 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain E 442–502（61 aa） Fragment：UNP residues 26-355,442-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ACH ACETYLCHOLINE × 2 CA CALCIUM ION × 3 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
8ST4 The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine Deposited 2023-05-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain B 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain B 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain C 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain C 442–502（61 aa） Fragment：UNP residues 26-355,442-502 Chain E 26–355（330 aa） Fragment：UNP residues 26-355,442-502 Chain E 442–502（61 aa） Fragment：UNP residues 26-355,442-502	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ACH ACETYLCHOLINE × 2 NA SODIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.35 Å

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHB2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–103； UniProt 231–330 Author chain A； PDBConstruct 109–137； UniProt 458–486

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	2lm2
Deposition date deposition_date	2011-11-18
Structure title title	NMR structures of the transmembrane domains of the AChR b2 subunit
Keywords keywords	Acetylcholine receptor, Transmembrane domain, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	19.18 Å
Radius of gyration Rg (electron density) rg_electron	18.32 Å
Forward intensity I(0) i0	986145000.00
Molecular weight molecular_weight	299360.0 kDa
Excluded volume excluded_volume	387470 Å³
Envelope volume envelope_volume	52357 Å³
Hydration-shell volume shell_volume	20548 Å³
Envelope diameter envelope_diameter	79.3 Å
Shell Rg shell_rg	28.54 Å
Envelope Rg envelope_rg	22.88 Å
Shape Rg shape_rg	18.36 Å
Total Rg total_rg	18.38 Å
Total atoms total_atoms	42660
Residues n_residues	2720
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	51.7 Å
Rg (real space) rg_real	18.05 Å
Rg uncertainty (real space) rg_real_error	0.09 Å
I(0) (real space) i0_real	9.4140e+08
I(0) uncertainty (real space) i0_real_error	8.4960e+06
Rg (reciprocal space) rg_reciprocal	19.40 Å
I(0) (reciprocal space) i0_reciprocal	986100000.0000
Solution quality estimate total_estimate	0.6668
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	18.0 Å
Skewness Skewness skewness	0.399
Kurtosis Kurtosis kurtosis	-0.472
Angular range angular_range	— – 0.4150 Å⁻¹
Current regularization parameter α current_alpha	3.1130
Highest regularization parameter α highest_alpha	678600.0000
Real-space data points n_real_points	73
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.904; Stabil: 0.990; Sysdev: 0.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2lm2A01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

▶

8. Citations (1)

▶

Description description	Neuronal acetylcholine receptor subunit beta-2
Molecular weight formula_weight	15085.8 kDa
Mutation mutation	R231E, R232E, K233E, L292S, V294S, L296S, K299E, T327E
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	42660

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	Escherichia coli

fit	/app/data/saxs_computation/lm/2lm2/2lm2.fit
pddf	/app/data/pr_computation/lm/2lm2/2lm2.pr.out
profile	/app/data/saxs_computation/lm/2lm2/2lm2.dat

NMR structures of the transmembrane domains of the AChR b2 subunit

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

Neuronal acetylcholine receptor subunit beta-2

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)