9nx0

Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI

Method: ELECTRON MICROSCOPY D_max: 152.2 Å Quality: GOOD

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

Alpha-conotoxin ImI

OrganismNot specified

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 × 10 其他Polymer 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain F； UniProt 5–16 Chain G； UniProt 5–16 Chain H； UniProt 5–16 Chain I； UniProt 5–16 Chain J； UniProt 5–16	Fragment：residues 5-16 Non-standard monomer：Yes (specific site not provided by mmCIF)	Neuronal acetylcholine receptor subunit alpha-7 × 5 （P36544） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.06 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 9NX0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CNL ALPHA-CONOTOXIN IMI Deposited 1999-05-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.1；280 K NMR sample composition 10% D2O/90% H2O	Resolution not provided
1E74 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT R11E Deposited 2000-08-24	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 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.1；298 K	Resolution not provided
1E75 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT R7L Deposited 2000-08-24	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 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.7；298 K	Resolution not provided
1E76 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 POINT MUTATION VARIANT D5N Deposited 2000-08-24	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 1–12（12 aa）	Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.1；298 K	Resolution not provided
1G2G MINIMAL CONFORMATION OF THE ALPHA-CONOTOXIN IMI FOR THE ALPHA7 NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR RECOGNITION Deposited 2000-10-19	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 1–12（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 5-6 mM alpha-ImI; 90 % H2O, 10 % D2O; 0.1 M potassium phosphate buffer pH 5.8 \| 90 % H2O, 10 % D2O; 0.1 M potassium phosphate buffer pH 5.8	Resolution not provided
1IM1 NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1, 20 STRUCTURES Deposited 1998-11-18	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 1–12（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3；298 K NMR sample composition 90% H2O/10% D2O OR 100% D2O	Resolution not provided
1IMI SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IM1 Deposited 1998-11-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–12（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；278 K；Pressure 1 NMR sample composition 90% H2O/ 10% D2O	Resolution not provided
2BC7 Solution structure of [Sec2,8]-ImI Deposited 2005-10-18	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 5–16（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；290 K；Ionic strength (raw mmCIF value) 1；Pressure ambient NMR sample composition 1mM peptide \| 90% H2O/10% D2O	Resolution not provided
2BC8 [Sec2,3,8,12]-ImI Deposited 2005-10-18	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 5–16（12 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.5；290 K；Ionic strength (raw mmCIF value) 1；Pressure ambient NMR sample composition 2mM [Sec2,3,8,12]-ImI \| 90% D2O, 10% H2O NMR sample composition 2mM [Sec2,3,8,12]-ImI \| 100% D2O	Resolution not provided
2BYP Crystal structure of Aplysia californica AChBP in complex with alpha- conotoxin ImI Deposited 2005-08-03	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain F 5–16（12 aa） Chain G 5–16（12 aa） Chain H 5–16（12 aa） Chain I 5–16（12 aa） Chain J 5–16（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；11-14% PEG-4000, 0.1 M TRIS, PH 7.5, 0.4 M MGCL2	Resolution 2.07 Å R-free 0.214
2C9T Crystal Structure Of Acetylcholine Binding Protein (AChBP) From Aplysia Californica In Complex With alpha-Conotoxin ImI Deposited 2005-12-14	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 × 18 PDB declaration: octadecameric	Chain K 5–16（12 aa） Fragment：RESIDUES 5-16 Chain M 5–16（12 aa） Fragment：RESIDUES 5-16 Chain O 5–16（12 aa） Fragment：RESIDUES 5-16 Chain P 5–16（12 aa） Fragment：RESIDUES 5-16 Chain Q 5–16（12 aa） Fragment：RESIDUES 5-16 Chain R 5–16（12 aa） Fragment：RESIDUES 5-16 Chain S 5–16（12 aa） Fragment：RESIDUES 5-16 Chain T 5–16（12 aa） Fragment：RESIDUES 5-16	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions 100 MM SODIUM ACETATE PH 5.5, 12.5% PEG5000 MME	Resolution 2.25 Å R-free 0.227
2MOA Solution NMR structure of peptide ImI1 (peak 2) Deposited 2014-04-24	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 5–16（12 aa） Fragment：UNP residues 5-16	Mutation：C2(81S), C3A Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.8；278 K；Ionic strength (raw mmCIF value) 0.1；Pressure ambient NMR sample composition 1 mM ImI1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CA1_CONIM
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain F； PDBConstruct 1–12； UniProt 5–16 Author chain G； PDBConstruct 1–12； UniProt 5–16 Author chain H； PDBConstruct 1–12； UniProt 5–16 Author chain I； PDBConstruct 1–12； UniProt 5–16 Author chain J； PDBConstruct 1–12； UniProt 5–16

Neuronal acetylcholine receptor subunit alpha-7

Homo sapiens

UniProt P36544

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 × 10 其他Polymer 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 24–501 Chain B； UniProt 24–501 Chain C； UniProt 24–501 Chain D； UniProt 24–501 Chain E； UniProt 24–501	Not recorded	Alpha-conotoxin ImI × 5 （P50983） 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.06 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 9NX0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2MAW NMR structures of the alpha7 nAChR transmembrane domain. Deposited 2013-07-19	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 228–326（99 aa） Fragment：UNP residues 141-235, transmembrane domain Chain A 467–496（30 aa） Fragment：UNP residues 141-235, transmembrane domain	Mutation：A195S, V200S, L202S Mutation：A195S, V200S, L202S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 0.01；Pressure ambient NMR sample composition 0.25 mM [U-100% 13C; U-100% 15N] protein, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
7EKI human alpha 7 nicotinic acetylcholine receptor in apo-form Deposited 2021-04-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CLR CHOLESTEROL × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
7EKP human alpha 7 nicotinic acetylcholine receptor bound to EVP-6124 Deposited 2021-04-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	I33 7-chloro-N-(quinuclidin-3-yl)benzo[b]thiophene-2-carboxamide × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CLR CHOLESTEROL × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.85 Å
7EKT human alpha 7 nicotinic acetylcholine receptor bound to EVP-6124 and PNU-120596 Deposited 2021-04-06	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CLR CHOLESTEROL × 5 I33 7-chloro-N-(quinuclidin-3-yl)benzo[b]thiophene-2-carboxamide × 5 I34 N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.02 Å
7KOO Alpha-7 nicotinic acetylcholine receptor bound to alpha-bungarotoxin in a resting state Deposited 2020-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–371（348 aa） Chain A 407–502（96 aa） Chain B 24–371（348 aa） Chain B 407–502（96 aa） Chain C 24–371（348 aa） Chain C 407–502（96 aa） Chain D 24–371（348 aa） Chain D 407–502（96 aa） Chain E 24–371（348 aa） Chain E 407–502（96 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
7KOQ Alpha-7 nicotinic acetylcholine receptor bound to epibatidine in a desensitized state Deposited 2020-11-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–371（348 aa） Chain A 407–502（96 aa） Chain B 24–371（348 aa） Chain B 407–502（96 aa） Chain C 24–371（348 aa） Chain C 407–502（96 aa） Chain D 24–371（348 aa） Chain D 407–502（96 aa） Chain E 24–371（348 aa） Chain E 407–502（96 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 EPJ EPIBATIDINE × 5 CA CALCIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7KOX Alpha-7 nicotinic acetylcholine receptor bound to epibatidine and PNU-120596 in the activated state Deposited 2020-11-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–371（348 aa） Chain A 407–502（96 aa） Chain B 24–371（348 aa） Chain B 407–502（96 aa） Chain C 24–371（348 aa） Chain C 407–502（96 aa） Chain D 24–371（348 aa） Chain D 407–502（96 aa） Chain E 24–371（348 aa） Chain E 407–502（96 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 EPJ EPIBATIDINE × 5 CA CALCIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
7RPM Structures of the Intracellular Domain and Transmembrane Domain of the Human alpha7 Nicotinic Acetylcholine Receptors Deposited 2021-08-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain B 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain C 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain D 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain E 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496	Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；308 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；298 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；298 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；298 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；298 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR sample composition 0.24 mM [U-13C; U-15N] alpha7nAChR TMD+ICD, 5 mM sodium acetate, 66 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] S358C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C375-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 66 mM LDAO, 20 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] C390-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] L415C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C427-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C435-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.28 mM V311C-MTSL alpha7 TMD-ICD, 0.07 mM [U-15N] V311C alpha7 TMD-ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.24 mM C427-MTSL alpha7 TMD-ICD, 0.06 mM [U-15N] C427 alpha7 TMD-ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.28 mM V311C alpha7 TMD-ICD, 0.07 mM [U-15N] V311C-MTSL alpha7 TMD-ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.24 mM C427 alpha7 TMD-ICD, 0.06 mM [U-15N] C427-MTSL alpha7 TMD-ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-13C; U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C427-EDTA-Lu3+ alpha7 TMD-ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C427-EDTA-Tm3+ alpha7 TMD-ICD, 5 mM sodium acetate, 66 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C317-EDTA-Lu3+ alpha7 TMD-ICD, 5 mM sodium acetate, 66 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C317-EDTA-Tm3+ alpha7 TMD-ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.24 mM [U-15N] C219-EDTA-Lu3+ alpha7 TMD-ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] C219-EDTA-Tm3+ alpha7 TMD-ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.35 mM [U-13C; U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-13C; U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.35 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 66 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] V311C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] C317-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.3 mM [U-15N] C335-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.3 mM [U-15N] C342-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 66 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.3 mM [U-15N] S350C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 53 mM LDAO, 25 mM NaCl, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
8C9X human alpha7 nicotinic receptor in complex with the C4 nanobody Deposited 2023-01-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–347（324 aa） Chain A 455–502（48 aa） Chain B 24–347（324 aa） Chain B 455–502（48 aa） Chain C 24–347（324 aa） Chain C 455–502（48 aa） Chain D 24–347（324 aa） Chain D 455–502（48 aa） Chain E 24–347（324 aa） Chain E 455–502（48 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8CAU human alpha7 nicotinic receptor in complex with the C4 nanobody and nicotine Deposited 2023-01-24	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–502（479 aa） Chain B 24–502（479 aa） Chain C 24–502（479 aa） Chain D 24–502（479 aa） Chain E 24–502（479 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8CE4 Human alpha7 nicotinic receptor in complex with the E3 nanobody Deposited 2023-02-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–347（324 aa） Chain A 455–502（48 aa） Chain B 24–347（324 aa） Chain B 455–502（48 aa） Chain C 24–347（324 aa） Chain C 455–502（48 aa） Chain D 24–347（324 aa） Chain D 455–502（48 aa） Chain E 24–347（324 aa） Chain E 455–502（48 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8CI1 Human alpha7 nicotinic receptor in complex with the E3 nanobody and nicotine Deposited 2023-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–347（324 aa） Chain A 455–502（48 aa） Chain B 24–347（324 aa） Chain B 455–502（48 aa） Chain C 24–347（324 aa） Chain C 455–502（48 aa） Chain D 24–347（324 aa） Chain D 455–502（48 aa） Chain E 24–347（324 aa） Chain E 455–502（48 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8CI2 human alpha7 nicotinic receptor in complex with the C4 nanobody under sub-saturating conditions Deposited 2023-02-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 8 PDB declaration: octameric	Chain A 24–347（324 aa） Chain A 455–502（48 aa） Chain B 24–347（324 aa） Chain B 455–502（48 aa） Chain C 24–347（324 aa） Chain C 455–502（48 aa） Chain D 24–347（324 aa） Chain D 455–502（48 aa） Chain E 24–347（324 aa） Chain E 455–502（48 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.40 Å
8F4V Alpha7 nicotinic acetylcholine receptor intracellular and transmembrane domains bound to ivermectin in a desensitized state Deposited 2022-11-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain B 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain C 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain D 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496 Chain E 231–496（266 aa） Fragment：Transmembrane domain and intracellular domain residues 231-496	Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E Mutation：A263S, V268S, L270S, A474E	IVM (2aE,4E,5'S,6S,6'R,7S,8E,11R,13R,15S,17aR,20R,20aR,20bS)-6'-[(2S)-butan-2-yl]-20,20b-dihydroxy-5',6,8,19-tetramethyl-17 -oxo-3',4',5',6,6',10,11,14,15,17,17a,20,20a,20b-tetradecahydro-2H,7H-spiro[11,15-methanofuro[4,3,2-pq][2,6]benzodioxacy clooctadecine-13,2'-pyran]-7-yl 2,6-dideoxy-4-O-(2,6-dideoxy-3-O-methyl-alpha-L-arabino-hexopyranosyl)-3-O-methyl-alpha-L-arabino-hexopyranoside × 5	SOLUTION NMR NMR measurement conditions pH 4.7；318 K；Ionic strength (raw mmCIF value) 25；Pressure 1 NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] V311C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 220 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] V311C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] C335-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 26 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 220 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-15N] C335-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 26 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C342-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 26 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 200 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 % [U-15N] C342-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 26 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] S350C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 200 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] S350C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C375-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 200 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C375-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 30 uM ivermectin, 0.1 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C390-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 250 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] C390-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.24 mM [U-15N] L415C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 240 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.24 mM [U-15N] L415C-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C435-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 22 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 200 uM ivermectin, 0.4 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.2 mM [U-15N] C435-MTSL alpha7nAChR TMD+ICD, 5 mM sodium acetate, 22 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-13C; U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 30 uM ivermectin, 30 uM PNU, 0.2 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.22 mM [U-13C; U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 44 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 100 uM ivermectin, 0.3 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 250 uM ivermectin, 0.55 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 500 uM ivermectin, 0.95 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 500 uM ivermectin, 0.8 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 500 uM ivermectin, 0.8 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.25 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 500 uM ivermectin, 0.8 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.20 mM [U-15N] alpha7nAChR C317 TMD+ICD, 5 mM sodium acetate, 35 mM LDAO, 25 mM sodium chloride, 5 % D2O, 20 uM DSS, 500 uM ivermectin, 0.8 % DMSO, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
8P1H Crystal structure of the chimera of human 14-3-3 zeta and phosphorylated cytoplasmic loop fragment of the alpha7 acetylcholine receptor Deposited 2023-05-12	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 Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 361–372（12 aa） Chain B 361–372（12 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 4 AZI AZIDE ION × 3 BEZ BENZOIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；288 K；0.2 M Magnesium acetate tetrahydrate; 0.1 M Sodium cacodylate trihydrate pH 6.5; 20% w/v Polyethylene glycol 8,000	Resolution 1.95 Å R-free 0.253
8UT1 Alpha7-nicotinic acetylcholine receptor bound to epibatidine Deposited 2023-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 15 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8UTB Alpha7-nicotinic acetylcholine receptor bound to epibatidine and NS-1738 Deposited 2023-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	XG3 N-(5-chloro-2-hydroxyphenyl)-N'-[2-chloro-5-(trifluoromethyl)phenyl]urea × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 EPJ EPIBATIDINE × 5 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8UZJ Alpha7-nicotinic acetylcholine receptor bound to epibatidine and ivermectin Deposited 2023-11-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5 IVM (2aE,4E,5'S,6S,6'R,7S,8E,11R,13R,15S,17aR,20R,20aR,20bS)-6'-[(2S)-butan-2-yl]-20,20b-dihydroxy-5',6,8,19-tetramethyl-17 -oxo-3',4',5',6,6',10,11,14,15,17,17a,20,20a,20b-tetradecahydro-2H,7H-spiro[11,15-methanofuro[4,3,2-pq][2,6]benzodioxacy clooctadecine-13,2'-pyran]-7-yl 2,6-dideoxy-4-O-(2,6-dideoxy-3-O-methyl-alpha-L-arabino-hexopyranosyl)-3-O-methyl-alpha-L-arabino-hexopyranoside × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8V80 Alpha7-nicotinic acetylcholine receptor bound to epibatidine and (-)-TQS Deposited 2023-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 10 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5 YLR (3aR,4S,9bS)-4-(naphthalen-1-yl)-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-8-sulfonamide × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.34 Å
8V82 Alpha7-nicotinic acetylcholine receptor bound to epibatidine and PNU-120596 Deposited 2023-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 15 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5 I34 N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
8V86 Alpha7-nicotinic acetylcholine receptor bound to GAT107 Deposited 2023-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 10 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 YLI (3aR,4S,9bS)-4-(4-bromophenyl)-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-8-sulfonamide × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.47 Å
8V88 Alpha7-nicotinic acetylcholine receptor bound to epibatidine and GAT107 Deposited 2023-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 10 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5 YLI (3aR,4S,9bS)-4-(4-bromophenyl)-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-8-sulfonamide × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8V89 Alpha7-nicotinic acetylcholine receptor time resolved resting state Deposited 2023-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 R16 HEXADECANE × 5 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.53 Å
8V8A Alpha7-nicotinic acetylcholine receptor time resolved bound to epibatidine and PNU-120596 desensitized intermediate state Deposited 2023-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 15 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 5 EPJ EPIBATIDINE × 5 I34 N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å
8V8C Alpha7-nicotinic acetylcholine receptor time resolved bound to epibatidine and PNU-120596 asymmetric state 1 Deposited 2023-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 EPJ EPIBATIDINE × 5 I34 N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea × 5 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.29 Å
8V8D Alpha7-nicotinic acetylcholine receptor time resolved bound to epibatidine and PNU-120596 asymmetric state 2 Deposited 2023-12-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 24–412（389 aa） Chain A 413–502（90 aa） Chain B 24–412（389 aa） Chain B 413–502（90 aa） Chain C 24–412（389 aa） Chain C 413–502（90 aa） Chain D 24–412（389 aa） Chain D 413–502（90 aa） Chain E 24–412（389 aa） Chain E 413–502（90 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 EPJ EPIBATIDINE × 5 I34 N-(5-Chloro-2,4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea × 5 CA CALCIUM ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
9IIR human alpha 7 nicotinic acetylcholine receptor in complex with GAT107 and calcium (desensitized state) Deposited 2024-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	YLI (3aR,4S,9bS)-4-(4-bromophenyl)-3a,4,5,9b-tetrahydro-3H-cyclopenta[c]quinoline-8-sulfonamide × 5 CA CALCIUM ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 CLR CHOLESTEROL × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
9IIV human alpha 7 nicotinic acetylcholine receptor in complex with GAT107 and calcium (open state) Deposited 2024-06-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 CA CALCIUM ION × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.89 Å
9J37 Cryo-EM structure of human Alpha-7 nicotinic acetylcholine receptor Deposited 2024-08-08	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 23–502（480 aa） Chain B 23–502（480 aa） Chain C 23–502（480 aa） Chain D 23–502（480 aa） Chain E 23–502（480 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CLR CHOLESTEROL × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9LH5 human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (open state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.61 Å
9LH6 human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (five-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
9LH8 human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (four-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
9LH9 human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (ortho-three-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.98 Å
9LHA human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (meta-three-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.96 Å
9LHB human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (ortho-two-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.11 Å
9LHC human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (meta-two-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.17 Å
9LHD human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (one-nicotine-bound desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
9LHE human alpha 7 nicotinic acetylcholine receptor in complex with L-nicotine (nicotine-free desensitized state) Deposited 2025-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å
9LN7 Alpha-7 nicotinic acetylcholine receptor bound to inhibitory bicyclic peptide KP2007 in a resting state. Deposited 2025-01-20	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 1–502（502 aa） Chain C 1–502（502 aa） Chain E 1–502（502 aa） Chain G 1–502（502 aa） Chain I 1–502（502 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
9NX1 Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImII Deposited 2025-03-25	Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 24–501（478 aa） Chain C 24–501（478 aa） Chain D 24–501（478 aa） Chain E 24–501（478 aa） Chain F 24–501（478 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 EPJ EPIBATIDINE × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9QTN Human alpha7 nicotinic receptor in complex with the F1 nanobody Deposited 2025-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–502（479 aa） Chain B 24–502（479 aa） Chain C 24–502（479 aa） Chain D 24–502（479 aa） Chain E 24–502（479 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.28 Å
9QTO Human alpha7 nicotinic receptor in complex with the E6 nanobody Deposited 2025-04-09	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 10 PDB declaration: decameric	Chain A 24–349（326 aa） Chain B 24–349（326 aa） Chain C 24–349（326 aa） Chain D 24–349（326 aa） Chain E 24–349（326 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.16 Å
9VIQ human alpha 7 nicotinic acetylcholine receptor L277A mutant in complex with L-nicotine (desensitized state) Deposited 2025-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Mutation：L277A Mutation：L277A Mutation：L277A Mutation：L277A Mutation：L277A	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.24 Å
9VIX human alpha 7 nicotinic acetylcholine receptor L278A mutant in complex with L-nicotine (desensitized state) Deposited 2025-06-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 1–502（502 aa） Chain B 1–502（502 aa） Chain C 1–502（502 aa） Chain D 1–502（502 aa） Chain E 1–502（502 aa）	Mutation：L278A Mutation：L278A Mutation：L278A Mutation：L278A Mutation：L278A	NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.06 Å

44 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACHA7_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–478； UniProt 24–501 Author chain B； PDBConstruct 1–478； UniProt 24–501 Author chain C； PDBConstruct 1–478； UniProt 24–501 Author chain D； PDBConstruct 1–478； UniProt 24–501 Author chain E； PDBConstruct 1–478； UniProt 24–501

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	9nx0
Deposition date deposition_date	2025-03-25
Structure title title	Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI
Keywords keywords	ion channel, toxin, MEMBRANE PROTEIN; 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	44.77 Å
Radius of gyration Rg (electron density) rg_electron	44.39 Å
Forward intensity I(0) i0	762091000.00
Molecular weight molecular_weight	238860.0 kDa
Excluded volume excluded_volume	303180 Å³
Envelope volume envelope_volume	409480 Å³
Hydration-shell volume shell_volume	77319 Å³
Envelope diameter envelope_diameter	162.1 Å
Shell Rg shell_rg	48.54 Å
Envelope Rg envelope_rg	44.76 Å
Shape Rg shape_rg	44.40 Å
Total Rg total_rg	44.55 Å
Total atoms total_atoms	32815
Residues n_residues	2020
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	152.2 Å
Rg (real space) rg_real	45.03 Å
Rg uncertainty (real space) rg_real_error	1.93 Å
I(0) (real space) i0_real	7.6210e+08
I(0) uncertainty (real space) i0_real_error	1.4010e+07
Rg (reciprocal space) rg_reciprocal	44.78 Å
I(0) (reciprocal space) i0_reciprocal	761900000.0000
Solution quality estimate total_estimate	0.8279
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	47.8 Å
Skewness Skewness skewness	0.575
Kurtosis Kurtosis kurtosis	-0.059
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	115000000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.703; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.678

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Alpha-conotoxin ImI
Molecular weight formula_weight	1356.6 kDa
Source method src_method	syn
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,H,I,J,F
Atom count atom_count	32885

GCCSDPRCAWRCX

Entity 2 Entity 2 polymer

Description description	Neuronal acetylcholine receptor subunit alpha-7
Molecular weight formula_weight	54120.4 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

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

EFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLNLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNPSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDF

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 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	424.4 kDa
Source method src_method	man
Copy count entity_count	10

Entity 4 Entity 4 non-polymer

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	221.2 kDa
Source method src_method	man
Copy count entity_count	5

Entity 5 Entity 5 non-polymer

Description description	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
Molecular weight formula_weight	760.1 kDa
Source method src_method	syn
Copy count entity_count	5

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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	3.060 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.06 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	80193

fit	/app/data/saxs_computation/nx/9nx0/9nx0.fit
pddf	/app/data/pr_computation/nx/9nx0/9nx0.pr.out
profile	/app/data/saxs_computation/nx/9nx0/9nx0.dat

Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI

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

Alpha-conotoxin ImI

State in the Current Structure

Other States of the Same Protein in the Database

Neuronal acetylcholine receptor subunit alpha-7

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

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 branched

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)