SAXSdb — 2bg9

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

ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN

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	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain A； UniProt 25–330 Chain A； UniProt 398–461 Chain D； UniProt 25–330 Chain D； UniProt 398–461	Not recorded	ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN × 1 （Q6S3I0） ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN × 1 （Q6S3H8） ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions：LIQUID ETHANE	Resolution 4.00 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 2BG9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1L4W NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin Deposited 2002-03-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 206–226（21 aa） Fragment：Acetylcholine receptor peptide (residues 206-226)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；303 K；Ionic strength (raw mmCIF value) 50 mM Ac；Pressure ambient NMR sample composition 1.8 mM alpha-Bungarotoxin/AChR-peptide, buffer,pH 4 \| 90% H2O/10% D2O NMR sample composition 1.8 mM alpha-Bungarotoxin/AChR-peptide, buffer,pH 4 \| 100% D2O	Resolution not provided
1LJZ NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin Deposited 2002-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 206–226（21 aa） Fragment：Acetylcholine receptor peptide (residues 182-202)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4；298 K；Ionic strength (raw mmCIF value) 50 mM NH4Ac；Pressure ambient NMR measurement conditions pH 4；298 K；Ionic strength (raw mmCIF value) 50 mM NH4Ac；Pressure ambient NMR sample composition acetylcholine receptor peptide/alpha-bungarotoxin \| 90% H2O/10% D2O NMR sample composition acetylcholine receptor peptide/alpha-bungarotoxin \| 100% D2O	Resolution not provided
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 235–461（227 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 235-461 Chain D 235–461（227 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 235-461	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOG The structure and super-organization of acetylcholine receptor-rapsyn complexes Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 2 1–461（461 aa） Chain A 1–461（461 aa） Chain D 1–461（461 aa） Chain F 1–461（461 aa） Chain I 1–461（461 aa） Chain K 1–461（461 aa） Chain N 1–461（461 aa） Chain P 1–461（461 aa） Chain S 1–461（461 aa） Chain U 1–461（461 aa） Chain X 1–461（461 aa） Chain Z 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 50.00 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–461（461 aa） Chain D 1–461（461 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

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

View Construct and Data Evidence

UniProt name	ACHA_TORMA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–306； UniProt 25–330 Author chain A； PDBConstruct 307–370； UniProt 398–461 Author chain D； PDBConstruct 1–306； UniProt 25–330 Author chain D； PDBConstruct 307–370； UniProt 398–461

ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN

OrganismNot specified

UniProt Q6S3I0

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain B； UniProt 25–188 Chain B； UniProt 198–336 Chain B； UniProt 427–493	Not recorded	ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN × 2 （P02711） ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN × 1 （Q6S3H8） ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions：LIQUID ETHANE	Resolution 4.00 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 2BG9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 241–490（250 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 241-490	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOG The structure and super-organization of acetylcholine receptor-rapsyn complexes Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 0 1–493（493 aa） Chain B 1–493（493 aa） Chain G 1–493（493 aa） Chain L 1–493（493 aa） Chain Q 1–493（493 aa） Chain V 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 50.00 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–493（493 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3I0
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–164； UniProt 25–188 Author chain B； PDBConstruct 165–303； UniProt 198–336 Author chain B； PDBConstruct 304–370； UniProt 427–493

ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN

OrganismNot specified

UniProt Q6S3H8

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain C； UniProt 22–183 Chain C； UniProt 199–341 Chain C； UniProt 442–505	Not recorded	ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN × 2 （P02711） ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN × 1 （Q6S3I0） ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions：LIQUID ETHANE	Resolution 4.00 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 2BG9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 246–505（260 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 246-505	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOG The structure and super-organization of acetylcholine receptor-rapsyn complexes Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 1 1–522（522 aa） Chain C 1–522（522 aa） Chain H 1–522（522 aa） Chain M 1–522（522 aa） Chain R 1–522（522 aa） Chain W 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 50.00 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–522（522 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3H8
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–162； UniProt 22–183 Author chain C； PDBConstruct 163–305； UniProt 199–341 Author chain C； PDBConstruct 306–369； UniProt 442–505

ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN

OrganismNot specified

UniProt Q6S3H9

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain E； UniProt 18–181 Chain E； UniProt 189–332 Chain E； UniProt 432–493	Not recorded	ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN × 2 （P02711） ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN × 1 （Q6S3I0） ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN × 1 （Q6S3H8）	ELECTRON MICROSCOPY cryo-EM buffer：100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE cryo-EM vitrification conditions：LIQUID ETHANE	Resolution 4.00 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 2BG9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1OED STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES Deposited 2003-03-24	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 235–494（260 aa） Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 236-495	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer SODIUM CACODYLATE；pH 6.8 cryo-EM vitrification conditions LIQUID ETHANE	Resolution 4.00 Å
4AQ5 Gating movement in acetylcholine receptor analysed by time-resolved electron cryo-microscopy (closed class) Deposited 2012-04-12	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–505（488 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4AQ9 Gating movement in acetylcholine receptor analysed by time- resolved electron cryo-microscopy (open class) Deposited 2012-04-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–505（488 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE；pH 7；100MM SODIUM CACODYLATE, 1MM CALCIUM CHLORIDE cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 85 TEMPERATURE- 120 INSTRUMENT- HOMEMADE PLUNGER METHOD- BLOT UNTIL APPLIED DROPLET LOSES CONTACT WITH FILTER PAPER (INDICATED BY LOSS OF TRANSPARENCY TYPICALLY 6S) TIMERESOLVEDSTATE- VITRIFIED WITHIN 10MS OF EXPOSURE TO ACETYLCHOLINE (APPLIED AS THE GRID IS BEING PLUNGED USING A FINE FOCUSSED SPRAY POSITIONED ABOUT 1CM ABOVE THE ETHANE SURFACE) DETAILS- VITRIFICATION CARRIED OUT AT AN AMBIENT TEMPERATURE OF 8 DEGREES	Resolution 6.20 Å
4BOG The structure and super-organization of acetylcholine receptor-rapsyn complexes Deposited 2013-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric	Chain 3 1–505（505 aa） Chain E 1–505（505 aa） Chain J 1–505（505 aa） Chain O 1–505（505 aa） Chain T 1–505（505 aa） Chain Y 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；ETHANE	Resolution 50.00 Å
4BOI The structure and super-organization of acetylcholine receptor-rapsyn complexes class A Deposited 2013-05-20	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 41.00 Å
4BON The structure and super-organization of acetylcholine receptor-rapsyn complexes class B Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 40.00 Å
4BOO The structure and super-organization of acetylcholine receptor-rapsyn complexes class C Deposited 2013-05-21	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE	Resolution 42.00 Å
4BOR The structure and super-organization of acetylcholine receptor-rapsyn complexes class D Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 42.00 Å
4BOT The structure and super-organization of acetylcholine receptor- rapsyn complexes class E Deposited 2013-05-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 1–505（505 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L；pH 7.4；400 MM NACL, 20 MM PHOSPHATE BUFFER, LEUPEPTIN 0.3 MG/L, PEPSTATIN 1 MG/L cryo-EM vitrification conditions Cryogen ETHANE；VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 78, INSTRUMENT- HOMEMADE PLUNGER, METHOD- BLOT FROM THE CARBON SIDE,	Resolution 42.00 Å

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	Q6S3H9
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–164； UniProt 18–181 Author chain E； PDBConstruct 165–307； UniProt 189–332 Author chain E； PDBConstruct 308–370； UniProt 432–493

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2bg9
Deposition date deposition_date	2004-12-17
Structure title title	REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.
Keywords keywords	ION CHANNEL/RECEPTOR, ACETYLCHOLINE RECEPTOR, ION CHANNEL, ION TRANSPORT, POSTSYNAPTIC MEMBRANE, ION CHANNEL-RECEPTOR complex; ION CHANNEL/RECEPTOR
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	43.92 Å
Radius of gyration Rg (electron density) rg_electron	43.21 Å
Forward intensity I(0) i0	586036000.00
Molecular weight molecular_weight	211510.0 kDa
Excluded volume excluded_volume	269820 Å³
Envelope volume envelope_volume	375020 Å³
Hydration-shell volume shell_volume	73383 Å³
Envelope diameter envelope_diameter	162.5 Å
Shell Rg shell_rg	47.52 Å
Envelope Rg envelope_rg	43.05 Å
Shape Rg shape_rg	43.22 Å
Total Rg total_rg	43.42 Å
Total atoms total_atoms	14924
Residues n_residues	1849
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	153.1 Å
Rg (real space) rg_real	44.13 Å
Rg uncertainty (real space) rg_real_error	1.73 Å
I(0) (real space) i0_real	5.8600e+08
I(0) uncertainty (real space) i0_real_error	1.1940e+07
Rg (reciprocal space) rg_reciprocal	43.93 Å
I(0) (reciprocal space) i0_reciprocal	585900000.0000
Solution quality estimate total_estimate	0.6012
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	51.0 Å
Skewness Skewness skewness	0.591
Kurtosis Kurtosis kurtosis	0.152
Angular range angular_range	— – 0.1800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	77330000.0000
Real-space data points n_real_points	37
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.660; Stabil: 1.000; Sysdev: 0.032; Positv: 1.000; Valcen: 0.994; Smooth: 0.739

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN
Molecular weight formula_weight	42501.3 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,D
Atom count atom_count	14924

SEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLINVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTVLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIVTVVVINTHHRSPSTHSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Entity 2 Entity 2 polymer

Description description	ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN
Molecular weight formula_weight	42167.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

SVMEDTLLSVLFENYNPKVRPSQTVGDKVTVRVGLTLTSLLILNEKNEEMTTSVFLNLAWTDYRLQWDPAAYEGIKDLSIPSDDVWQPDIVLMNNNDGSFEITLHVNVLVQHTGAVSWHPSAIYRSSCTIKVMYFPFDWQNCTMVFKSYTYDTSEVILQHALDAMINQDAFTENGQWSIEHKPSRKNWRSDDPSYEDVTFYLIIQRKPLFYIVYTIVPCILISILAILVFYLPPDAGEKMSLSISALLALTVFLLLLADKVPETSLSVPIIISYLMFIMILVAFSVILSVVVLNLHHRSPNTHEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYIFITMCSIGTFSIFLDASHNVPPDNPFA

Entity 3 Entity 3 polymer

Description description	ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN
Molecular weight formula_weight	42280.7 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

VNEEERLINDLLIVNKYNKHVRPVKHNNEVVNIALSLTLSNLISLKETDETLTTNVWMDHAWYDHRLTWNASEYSDISILRLRPELIWIPDIVLQNNNDGQYNVAYFCNVLVRPNGYVTWLPPAIFRSSCPINVLYFPFDWQNCSLKFTALNYNANEISMDLIIDPEAFTENGEWEIIHKPAKKNIYGDKFPNGTNYQDVTFYLIIRRKPLFYVINFITPCVLISFLAALAFYLPAESGEKMSTAICVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVVVNCGIVLNFHFRTPSTHSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNRPPAK

Entity 4 Entity 4 polymer

Description description	ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN
Molecular weight formula_weight	42299.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

NEEGRLIEKLLGDYDKRIKPAKTLDHVIDVTLKLTLTNLISLNEKEEALTTNVWIEIQWNDYRLSWNTSEYEGIDLVRIPSELLWLPDVVLENNVDGQFEVAYYANVLVYNDGSMYWLPPAIYRSTCPIAVTYFPFDWQNCSLVFRSQTYNAHEVNLQLSAEEGIDPEDFTENGEWTIRHRPAKKNYNWQLTKDDIDFQEIIFFLIIQRKPLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSLVIVTNCVIVLNVSLRTPNTHSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSLGTLAIFLTGHLNQVPE

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7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	2bg9A01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	2bg9A02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	2bg9B01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	2bg9B02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	2bg9C01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	2bg9C02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	2bg9D01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	2bg9D02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

Domain ID domain_id	2bg9E01
Class class	2 — Mainly Beta
Architecture architecture	70 — Distorted Sandwich
Topology topology	170 — Acetylcholine Binding Protein; Chain: A,
Homologous superfamily homologous superfamily	10 — Neurotransmitter-gated ion-channel ligand-binding domain

Domain ID domain_id	2bg9E02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily	390 — Neurotransmitter-gated ion-channel transmembrane domain

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8. Citations (2)

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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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	4.00 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	—

fit	/app/data/saxs_computation/bg/2bg9/2bg9.fit
pddf	/app/data/pr_computation/bg/2bg9/2bg9.pr.out
profile	/app/data/saxs_computation/bg/2bg9/2bg9.dat

REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION.

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

ACETYLCHOLINE RECEPTOR PROTEIN, ALPHA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

ACETYLCHOLINE RECEPTOR PROTEIN, BETA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

ACETYLCHOLINE RECEPTOR PROTEIN, DELTA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

ACETYLCHOLINE RECEPTOR PROTEIN, GAMMA CHAIN

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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)