9qtn

Human alpha7 nicotinic receptor in complex with the F1 nanobody

Method: ELECTRON MICROSCOPY D_max: 117.3 Å Quality: GOOD

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

Neuronal acetylcholine receptor subunit alpha-7

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 × 10 其他Polymer 15 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 24–502 Chain B； UniProt 24–502 Chain C； UniProt 24–502 Chain D； UniProt 24–502 Chain E； UniProt 24–502	Not recorded	Nanobody F1 × 5 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 4 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 ;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.28 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 9QTN	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 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 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 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 experimental conditions 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 oligomeric state 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
9NX0 Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImI Deposited 2025-03-25	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 24–501（478 aa） Chain B 24–501（478 aa） Chain C 24–501（478 aa） Chain D 24–501（478 aa） Chain E 24–501（478 aa）	Not recorded	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
9NX1 Alpha7-nicotinic acetylcholine receptor bound to conotoxin ImII Deposited 2025-03-25	Different construct Different oligomeric state Different ligand/ion Different experimental conditions 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
9QTO Human alpha7 nicotinic receptor in complex with the E6 nanobody Deposited 2025-04-09	Different construct Different oligomeric state 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 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：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	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–479； UniProt 24–502 Author chain B； PDBConstruct 1–479； UniProt 24–502 Author chain C； PDBConstruct 1–479； UniProt 24–502 Author chain D； PDBConstruct 1–479； UniProt 24–502 Author chain E； PDBConstruct 1–479； UniProt 24–502

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	9qtn
Deposition date deposition_date	2025-04-09
Structure title title	Human alpha7 nicotinic receptor in complex with the F1 nanobody
Keywords keywords	Nicotinic receptor, Nanobody, 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	39.09 Å
Radius of gyration Rg (electron density) rg_electron	38.21 Å
Forward intensity I(0) i0	622156000.00
Molecular weight molecular_weight	204520.0 kDa
Excluded volume excluded_volume	255790 Å³
Envelope volume envelope_volume	347090 Å³
Hydration-shell volume shell_volume	72564 Å³
Envelope diameter envelope_diameter	127.6 Å
Shell Rg shell_rg	46.78 Å
Envelope Rg envelope_rg	37.43 Å
Shape Rg shape_rg	38.15 Å
Total Rg total_rg	38.89 Å
Total atoms total_atoms	14419
Residues n_residues	1695
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	117.3 Å
Rg (real space) rg_real	38.74 Å
Rg uncertainty (real space) rg_real_error	0.49 Å
I(0) (real space) i0_real	6.2220e+08
I(0) uncertainty (real space) i0_real_error	9.5080e+06
Rg (reciprocal space) rg_reciprocal	38.96 Å
I(0) (reciprocal space) i0_reciprocal	622300000.0000
Solution quality estimate total_estimate	0.8863
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	52.8 Å
Skewness Skewness skewness	0.068
Kurtosis Kurtosis kurtosis	-0.400
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	83760000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.847

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (9)

Entity 1 Entity 1 polymer

Description description	Neuronal acetylcholine receptor subunit alpha-7
Molecular weight formula_weight	54154.4 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E
Atom count atom_count	14522

EFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA

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	Nanobody F1
Molecular weight formula_weight	14355.0 kDa
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

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

EVQLVESGGGLVQAGGSLRLSCAAPGITLSRYGMYGMGWFRQAPGKEREFVAAITWSGGQTYYQDSVKGRFTISRDNAKKLTFLQMNSLKPEDTAVYYCAADGDRFYPEPVVDDNAYKFWGQGTQVTVSSA

来源 Source

来源生物 organism	Vicugna pacos
NCBI Class编号 ncbi_taxonomy_id	30538
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 branched

Description description	;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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	910.8 kDa
Source method src_method	man
Copy count entity_count	4

Entity 4 Entity 4 branched

Description description	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
Molecular weight formula_weight	570.5 kDa
Source method src_method	man
Copy count entity_count	6

Entity 5 Entity 5 branched

Description description	;alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ;
Molecular weight formula_weight	894.8 kDa
Source method src_method	man
Copy count entity_count	1

Entity 6 Entity 6 branched

Description description	;2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-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	951.9 kDa
Source method src_method	man
Copy count entity_count	1

Entity 7 Entity 7 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	2

Entity 8 Entity 8 branched

Description description	;alpha-D-mannopyranose-(1-3)-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	748.7 kDa
Source method src_method	man
Copy count entity_count	1

Entity 9 Entity 9 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	103

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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	triclinic

Resolution resolution	2.28 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	325670

fit	/app/data/saxs_computation/qt/9qtn/9qtn.fit
pddf	/app/data/pr_computation/qt/9qtn/9qtn.pr.out
profile	/app/data/saxs_computation/qt/9qtn/9qtn.dat

Human alpha7 nicotinic receptor in complex with the F1 nanobody

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

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (9)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 branched

Entity 4 Entity 4 branched

Entity 5 Entity 5 branched

Entity 6 Entity 6 branched

Entity 7 Entity 7 branched

Entity 8 Entity 8 branched

Entity 9 Entity 9 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)