8st3

The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium

Method: ELECTRON MICROSCOPY D_max: 193.0 Å Quality: REASONABLE

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

Neuronal acetylcholine receptor subunit alpha-4

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	Other combination Heteromer Protein × 11 其他Polymer 3 PDB declaration: undecameric（11） Consistent with protein copy count	Chain A； UniProt 27–364 Chain A； UniProt 582–627 Chain D； UniProt 27–364 Chain D； UniProt 582–627	Fragment：UNP residues 27-364,582-627	Neuronal acetylcholine receptor subunit beta-2 × 3 （P17787） IgG1 Kappa Light Chain × 3 IgG1 Heavy Chain × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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

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 8ST3	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LLY NMR structures of the transmembrane domains of the nAChR a4 subunit Deposited 2011-11-18	Different construct Different mutation/modification Different oligomeric state 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 240–339（100 aa） Fragment：Helical transmembrane region, residues 242-339 and residues 598-625 Chain A 598–626（29 aa） Fragment：Helical transmembrane region, residues 242-339 and residues 598-625	Mutation：R240E, R241E, L301S, I303S, L305S, R336E, M626E Mutation：R240E, R241E, L301S, I303S, L305S, R336E, M626E	No recorded non-water small molecule	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, 10 mM sodium chloride, 5 % [U-100% 2H] D2O, 0.1 mM DSS, 10 mM sodium chloride, 20 mM beta-mercaptoethanol, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
5KXI X-ray structure of the human Alpha4Beta2 nicotinic receptor Deposited 2016-07-20	Different construct 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 27–364（338 aa） Fragment：UNP residues 27-364, 586-627,UNP residues 27-364, 586-627 Chain A 586–627（42 aa） Fragment：UNP residues 27-364, 586-627,UNP residues 27-364, 586-627 Chain D 27–364（338 aa） Fragment：UNP residues 27-364, 586-627,UNP residues 27-364, 586-627 Chain D 586–627（42 aa） Fragment：UNP residues 27-364, 586-627,UNP residues 27-364, 586-627	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 ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 27–364（338 aa） Chain A 586–627（42 aa） Chain D 27–364（338 aa） Chain D 586–627（42 aa）	Mutation：Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit Mutation：Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit Mutation：Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit Mutation：Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 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 conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 27–364（338 aa） Chain A 586–627（42 aa） Chain B 27–364（338 aa） Chain B 586–627（42 aa） Chain D 27–364（338 aa） Chain D 586–627（42 aa）	Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit ; Mutation：;Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 subunit,Glu-Arg linker was inserted in the MX-M4 junction, between Phe559-Ser560 in the alpha4 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 27–364（338 aa） Chain A 589–627（39 aa） Chain D 27–364（338 aa） Chain D 589–627（39 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 27–358（332 aa） Chain A 589–627（39 aa） Chain D 27–358（332 aa） Chain D 589–627（39 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 ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 27–627（601 aa） Chain D 27–627（601 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 ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 27–627（601 aa） Chain D 27–627（601 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 structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain A 582–627（46 aa） Fragment：UNP residues 27-364,582-627 Chain B 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain B 582–627（46 aa） Fragment：UNP residues 27-364,582-627 Chain D 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain D 582–627（46 aa） Fragment：UNP residues 27-364,582-627	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 structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain A 582–627（46 aa） Fragment：UNP residues 27-364,582-627 Chain B 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain B 582–627（46 aa） Fragment：UNP residues 27-364,582-627 Chain D 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain D 582–627（46 aa） Fragment：UNP residues 27-364,582-627	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
8ST4 The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine Deposited 2023-05-09	Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 11 PDB declaration: undecameric	Chain A 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain A 582–627（46 aa） Fragment：UNP residues 27-364,582-627 Chain D 27–364（338 aa） Fragment：UNP residues 27-364,582-627 Chain D 582–627（46 aa） Fragment：UNP residues 27-364,582-627	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

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHA4_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–338； UniProt 27–364 Author chain A； PDBConstruct 339–386； UniProt 582–627 Author chain D； PDBConstruct 1–338； UniProt 27–364 Author chain D； PDBConstruct 339–386； UniProt 582–627

Neuronal acetylcholine receptor subunit beta-2

Homo sapiens

UniProt P17787

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Other combination Heteromer Protein × 11 其他Polymer 3 PDB declaration: undecameric（11） Consistent with protein copy count	Chain B； UniProt 26–355 Chain B； UniProt 442–502 Chain C； UniProt 26–355 Chain C； UniProt 442–502 Chain E； UniProt 26–355 Chain E； UniProt 442–502	Fragment：UNP residues 26-355,442-502	Neuronal acetylcholine receptor subunit alpha-4 × 2 （P43681） IgG1 Kappa Light Chain × 3 IgG1 Heavy Chain × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 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

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 8ST3	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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	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 oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	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 oligomeric state 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 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
2LM2 NMR structures of the transmembrane domains of the AChR b2 subunit Deposited 2011-11-18	Different construct Different mutation/modification Different oligomeric state 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 231–330（100 aa） Fragment：Helical transmembrane region, residues 234-330 and residues 458-484 Chain A 458–486（29 aa） Fragment：Helical transmembrane region, residues 234-330 and residues 458-484	Mutation：R231E, R232E, K233E, L292S, V294S, L296S, K299E, T327E Mutation：R231E, R232E, K233E, L292S, V294S, L296S, K299E, T327E	No recorded non-water small molecule	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
5KXI X-ray structure of the human Alpha4Beta2 nicotinic receptor Deposited 2016-07-20	Different construct 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 ligand/ion 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 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 oligomeric state Different ligand/ion 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 oligomeric state Different ligand/ion 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 ligand/ion 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 ligand/ion 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 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 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
8ST4 The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine Deposited 2023-05-09	Different ligand/ion 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	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–330； UniProt 26–355 Author chain B； PDBConstruct 331–393； UniProt 442–502 Author chain C； PDBConstruct 1–330； UniProt 26–355 Author chain C； PDBConstruct 331–393； UniProt 442–502 Author chain E； PDBConstruct 1–330； UniProt 26–355 Author chain E； PDBConstruct 331–393； UniProt 442–502

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8st3
Deposition date deposition_date	2023-05-09
Structure title title	The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium
Keywords keywords	cys-loop ligand-gated pentameric ion channels, cation-selective channel, acetylcholine, calcium, TRANSPORT PROTEIN; TRANSPORT 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	55.52 Å
Radius of gyration Rg (electron density) rg_electron	54.67 Å
Forward intensity I(0) i0	1705240000.00
Molecular weight molecular_weight	359940.0 kDa
Excluded volume excluded_volume	456130 Å³
Envelope volume envelope_volume	638470 Å³
Hydration-shell volume shell_volume	100110 Å³
Envelope diameter envelope_diameter	202.3 Å
Shell Rg shell_rg	54.96 Å
Envelope Rg envelope_rg	55.08 Å
Shape Rg shape_rg	54.67 Å
Total Rg total_rg	54.68 Å
Total atoms total_atoms	50529
Residues n_residues	3155
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	193.0 Å
Rg (real space) rg_real	55.63 Å
Rg uncertainty (real space) rg_real_error	2.03 Å
I(0) (real space) i0_real	1.7050e+09
I(0) uncertainty (real space) i0_real_error	3.5650e+07
Rg (reciprocal space) rg_reciprocal	55.43 Å
I(0) (reciprocal space) i0_reciprocal	1705000000.0000
Solution quality estimate total_estimate	0.6356
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	68.9 Å
Skewness Skewness skewness	0.443
Kurtosis Kurtosis kurtosis	0.083
Angular range angular_range	— – 0.1400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	122700000.0000
Real-space data points n_real_points	29
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 1.000; Smooth: 0.702

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	Neuronal acetylcholine receptor subunit alpha-4
Molecular weight formula_weight	44862.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	50536

SSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVDTDFERSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI

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

Entity 2 Entity 2 polymer

Description description	Neuronal acetylcholine receptor subunit beta-2
Molecular weight formula_weight	46748.9 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,C,E

TDTEERLVEHLLDPSRYNKLIRPATNGSELVTVQLMVSLAQLISVHEREQIMTTNVWLTQEWEDYRLTWKPEEFDNMKKVRLPSKHIWLPDVVLYNNADGMYEVSFYSNAVVSYDGSIFWLPPAIYKSACKIEVKHFPFDQQNCTMKFRSWTYDRTEIDLVLKSEVASLDDFTPSGEWDIVALPGRRNENPDDSTYVDITYDFIIRRKPLFYTINLIIPCVLITSLAILVFYLPSDCGEKMTLCISVLLALTVFLLLISKIVPPTSLDVPLVGKYLMFTMVLVTFSIVTSVCVLNVHHRSPTTHTMAPWVKVVFLEKLPALLFMQQPRHHDDDQERSVSEDWKYVAMVIDRLFLWIFVFVCVFGTIGMFLQPLFQNYTTTTFLHSDHSAPSSKSAWSHPQFEK

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

Entity 3 Entity 3 polymer

Description description	IgG1 Kappa Light Chain
Molecular weight formula_weight	26378.6 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,H,J

MKLPVRLLVLMFWIPASSSDVLMTQTPLSLPVSLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPWTFGGGTKLEIKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Entity 4 Entity 4 polymer

Description description	IgG1 Heavy Chain
Molecular weight formula_weight	51195.7 kDa
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,I,K

MEWTWVFLFLLSVTAGVHSQVQLQQSGAEVMKPGASVKISCKGTGYTFSSYWIEWVKQRPGHGLERIGEILPGSGSTNYNEKFRGKATFTADKSSKTAYMQLSSLTSEDSAVYYCARYLPYYYAMDYWGQGTSVTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCGCKPCICTVPEVSSVFIFPPKPKDVLTITLTPKVTCVVVDISKDDPEVQFSWFVDDVEVHTAQTQPREEQFNSTFRSVSELPIMHQDWLNGKEFKCRVNSAAFPAPIEKTISKTKGRPKAPQVYTIPPPKEQMAKDKVSLTCMITDFFPEDITVEWQWNGQPAENYKNTQPIMDTDGSYFVYSKLNVQKSNWEAGNTFTCSVLHEGLHNHHTEKSLSHSPGK

Entity 5 Entity 5 branched

Description description	beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	586.5 kDa
Source method src_method	man
Copy count entity_count	3

Entity 6 Entity 6 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 7 Entity 7 non-polymer

Description description	ACETYLCHOLINE
Molecular weight formula_weight	146.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 8 Entity 8 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 9 Entity 9 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	7

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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	2.93 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	321064

fit	/app/data/saxs_computation/st/8st3/8st3.fit
pddf	/app/data/pr_computation/st/8st3/8st3.pr.out
profile	/app/data/saxs_computation/st/8st3/8st3.dat

The 2alpha3beta stoichiometry of human alpha4beta2 nicotinic acetylcholine receptor in complex with acetylcholine and calcium

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

Neuronal acetylcholine receptor subunit alpha-4

State in the Current Structure

Other States of the Same Protein in the Database

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

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 branched

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)