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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P02711 New Search
12PDB entries
12Biological assembly
34chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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
2BG9 REFINED STRUCTURE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR AT 4A RESOLUTION. Deposited 2004-12-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric（30） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.