SAXSdb — 1oed

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

Acetylcholine receptor subunit alpha

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 235–461 Chain D； UniProt 235–461	Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 235-461	Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor delta subunit × 1 （Q6S3H8） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：SODIUM CACODYLATE；pH 6.8 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 1OED	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
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 25–330（306 aa） Chain A 398–461（64 aa） Chain D 25–330（306 aa） Chain D 398–461（64 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE 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 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 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 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 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 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 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 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 1–227； UniProt 235–461 Author chain D； PDBConstruct 1–227； UniProt 235–461

Acetylcholine receptor beta subunit

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 241–490	Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 241-490	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor delta subunit × 1 （Q6S3H8） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：SODIUM CACODYLATE；pH 6.8 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 1OED	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 25–188（164 aa） Chain B 198–336（139 aa） Chain B 427–493（67 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE 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 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 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 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 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 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 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 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_TORMA
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–250； UniProt 241–490

Acetylcholine receptor delta subunit

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 246–505	Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 246-505	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor gamma subunit × 1 （Q6S3H9）	ELECTRON MICROSCOPY cryo-EM buffer：SODIUM CACODYLATE；pH 6.8 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 1OED	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 22–183（162 aa） Chain C 199–341（143 aa） Chain C 442–505（64 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE 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 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 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 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 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 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 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 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_TORMA
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–260； UniProt 246–505

Acetylcholine receptor gamma subunit

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 235–494	Fragment：MEMBRANE-SPANNING DOMAIN, RESIDUES 236-495	Acetylcholine receptor subunit alpha × 2 （P02711） Acetylcholine receptor beta subunit × 1 （Q6S3I0） Acetylcholine receptor delta subunit × 1 （Q6S3H8）	ELECTRON MICROSCOPY cryo-EM buffer：SODIUM CACODYLATE；pH 6.8 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 1OED	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17	Different construct Different mutation/modification Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain E 18–181（164 aa） Chain E 189–332（144 aa） Chain E 432–493（62 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 100MM SODIUM CACODYLATE；pH 6.8；100MM SODIUM CACODYLATE 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 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 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 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 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 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 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 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_TORMA
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–260； UniProt 235–494

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	1oed
Deposition date deposition_date	2003-03-24
Structure title title	STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES
Keywords keywords	ION CHANNEL/RECEPTOR, ION CHANNEL, TUBULAR CRYSTAL, ACETYLCHOLINE RECEPTOR, TRANSMEMBRANE, 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	27.31 Å
Radius of gyration Rg (electron density) rg_electron	25.91 Å
Forward intensity I(0) i0	58283200.00
Molecular weight molecular_weight	70009.0 kDa
Excluded volume excluded_volume	92317 Å³
Envelope volume envelope_volume	114340 Å³
Hydration-shell volume shell_volume	35796 Å³
Envelope diameter envelope_diameter	88.3 Å
Shell Rg shell_rg	34.12 Å
Envelope Rg envelope_rg	25.98 Å
Shape Rg shape_rg	25.92 Å
Total Rg total_rg	26.91 Å
Total atoms total_atoms	4926
Residues n_residues	636
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	84.7 Å
Rg (real space) rg_real	27.12 Å
Rg uncertainty (real space) rg_real_error	0.38 Å
I(0) (real space) i0_real	5.8280e+07
I(0) uncertainty (real space) i0_real_error	6.3900e+05
Rg (reciprocal space) rg_reciprocal	27.18 Å
I(0) (reciprocal space) i0_reciprocal	58290000.0000
Solution quality estimate total_estimate	0.8889
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	36.5 Å
Skewness Skewness skewness	0.147
Kurtosis Kurtosis kurtosis	-0.328
Angular range angular_range	— – 0.2900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	14500000.0000
Real-space data points n_real_points	59
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.971

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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 subunit alpha
Molecular weight formula_weight	25389.0 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	4926

PLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG

Entity 2 Entity 2 polymer

Description description	Acetylcholine receptor beta subunit
Molecular weight formula_weight	28387.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

PLFYIVYTIIPCILISILAILVFYLPPDAGEKMSLSISALLAVTVFLLLLADKVPETSLSVPIIIRYLMFIMILVAFSVILSVVVLNLHHRSPNTHTMPNWIRQIFIETLPPFLWIQRPVTTPSPDSKPTIISRANDEYFIRKPAGDFVCPVDNARVAVQPERLFSEMKWHLNGLTQPVTLPQDLKEAVEAIKYIAEQLESASEFDDLKKDWQYVAMVADRLFLYVFFVICSIGTFSIFLDASHNVPPDN

Entity 3 Entity 3 polymer

Description description	Acetylcholine receptor delta subunit
Molecular weight formula_weight	29371.1 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

PLFYVINFITPCVLISFLASLAFYLPAESGEKMSTAISVLLAQAVFLLLTSQRLPETALAVPLIGKYLMFIMSLVTGVIVNCGIVLNFHFRTPSTHVLSTRVKQIFLEKLPRILHMSRADESEQPDWQNDLKLRRSSSVGYISKAQEYFNIKSRSELMFEKQSERHGLVPRVTPRIGFGNNNENIAASDQLHDEIKSGIDSTNYIVKQIKEKNAYDEEVGNWNLVGQTIDRLSMFIITPVMVLGTIFIFVMGNFNHPPAK

Entity 4 Entity 4 polymer

Description description	Acetylcholine receptor gamma subunit
Molecular weight formula_weight	29321.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

PLFYIINIIAPCVLISSLVVLVYFLPAQAGGQKCTLSISVLLAQTIFLFLIAQKVPETSLNVPLIGKYLIFVMFVSMLIVMNCVIVLNVSLRTPNTHSLSEKIKHLFLGFLPKYLGMQLEPSEETPEKPQPRRRSSFGIMIKAEEYILKKPRSELMFEEQKDRHGLKRVNKMTSDIDIGTTVDLYKDLANFAPEIKSCVEACNFIAKSTKEQNDSGSENENWVLIGKVIDKACFWIALLLFSIGTLAIFLTGHFNQVPEF

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d1oeda_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedb_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedc_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oedd_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

Domain ID domain_id	d1oede_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.36 — Neurotransmitter-gated ion-channel transmembrane pore
Superfamily Superfamily superfamily	f.36.1 — Neurotransmitter-gated ion-channel transmembrane pore
Family Family family	f.36.1.1 — Neurotransmitter-gated ion-channel transmembrane pore

CATH v4.4 (5 domains)

Domain ID domain_id	1oedA00
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	1oedB00
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	1oedC00
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	1oedD00
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	1oedE00
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 (4)

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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/oe/1oed/1oed.fit
pddf	/app/data/pr_computation/oe/1oed/1oed.pr.out
profile	/app/data/saxs_computation/oe/1oed/1oed.dat

STRUCTURE OF ACETYLCHOLINE RECEPTOR PORE FROM ELECTRON IMAGES

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

Acetylcholine receptor subunit alpha

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor beta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor delta subunit

State in the Current Structure

Other States of the Same Protein in the Database

Acetylcholine receptor gamma subunit

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

SCOP 2.08 (5 domains)

CATH v4.4 (5 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)