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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：P47871 New Search
26PDB entries
30Biological assembly
36chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
3CZF Crystal structure of HLA-B*2709 complexed with the glucagon receptor (GR) peptide (residues 412-420) Deposited 2008-04-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 412–420（9 aa） Fragment：RESIDUES 412-420
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；291 K；14% (w/v) PEG 4000, 20mM Tris/HCl pH 7.5, 150mM NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 291K, pH 7.50
Resolution 1.20 Å R-free 0.149
4ERS A Molecular Basis for Negative Regulation of the Glucagon Receptor Deposited 2012-04-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 28–123（96 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；0.1M Tris pH 8.5, 0.2M sodium chloride, 25% (w/v) PEG3350, VAPOR DIFFUSION
Resolution 2.64 Å R-free 0.279
4ERS A Molecular Basis for Negative Regulation of the Glucagon Receptor Deposited 2012-04-20 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 28–123（96 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；0.1M Tris pH 8.5, 0.2M sodium chloride, 25% (w/v) PEG3350, VAPOR DIFFUSION
Resolution 2.64 Å R-free 0.279
4L6R Structure of the class B human glucagon G protein coupled receptor Deposited 2013-06-12 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 123–432（310 aa） Fragment：UNP residues 23-128 and 123-434
Mutation：M7W, H102I, R106L PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；293 K；100 mM MES pH 6.0, 140-200 mM NaK tartrate tetrahydrate, 9-17% (v/v) PEG 400, 0.35-0.55% (v/v) Jeffamine M-600 pH 7.0, 200 uM NNC0640, Lipidic Cubic Phase (LCP), temperature 293K
Resolution 3.30 Å R-free 0.339
4LF3 Inhibitory Mechanism of an Allosteric Antibody Targeting the Glucagon Receptor Deposited 2013-06-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 29–123（95 aa） Fragment：GCGR ECD (UNP residues 29-123)
Mutation：G40S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；289 K；0.1 M Tris-HCl, 0.2 M NaCl, PEG3350, pH 8.5, vapor diffusion, hanging drop, temperature 289K
Resolution 2.73 Å R-free 0.264
4LF3 Inhibitory Mechanism of an Allosteric Antibody Targeting the Glucagon Receptor Deposited 2013-06-26 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain F 29–123（95 aa） Fragment：GCGR ECD (UNP residues 29-123)
Mutation：G40S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；289 K；0.1 M Tris-HCl, 0.2 M NaCl, PEG3350, pH 8.5, vapor diffusion, hanging drop, temperature 289K
Resolution 2.73 Å R-free 0.264
5EE7 Crystal structure of the human glucagon receptor (GCGR) in complex with the antagonist MK-0893 Deposited 2015-10-22 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 136–254（119 aa）
Chain A 259–417（159 aa）
Mutation：;G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F ; Mutation：;G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F,G154A R173A A182L S190A G223A M276A E362F G207E K344A F387A V193F ; 5MV 3-[[4-[(1~{S})-1-[3-[3,5-bis(chloranyl)phenyl]-5-(6-methoxynaphthalen-2-yl)pyrazol-1-yl]ethyl]phenyl]carbonylamino]propanoic acid × 1 OLA OLEIC ACID × 14 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 6；293.15 K；ADA BUFFER, SODIUM POTASSIUM TARTRATE, PEG 400
Resolution 2.50 Å R-free 0.263
5XEZ Structure of the Full-length glucagon class B G protein-coupled receptor Deposited 2017-04-06 Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 27–256（230 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Chain A 260–432（173 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Mutation：C54T, C97A Mutation：C54T, C97A NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES, pH7.0, 300mM potassium phosphate monobasic, 25% PEG500DME, 100mM gly-gly-glycine
Resolution 3.00 Å R-free 0.243
5XEZ Structure of the Full-length glucagon class B G protein-coupled receptor Deposited 2017-04-06 Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 27–256（230 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Chain B 260–432（173 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Mutation：C54T, C97A Mutation：C54T, C97A NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES, pH7.0, 300mM potassium phosphate monobasic, 25% PEG500DME, 100mM gly-gly-glycine
Resolution 3.00 Å R-free 0.243
5XF1 Structure of the Full-length glucagon class B G protein-coupled receptor Deposited 2017-04-06 Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 27–256（230 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Chain A 260–432（173 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Mutation：C54T, C97A Mutation：C54T, C97A 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES, pH7.0, 200mM potassium phospphate monobasic, 20% PEG500DME, 10 mM gly-gly-glysine
Resolution 3.19 Å R-free 0.231
5XF1 Structure of the Full-length glucagon class B G protein-coupled receptor Deposited 2017-04-06 Assembly 2 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 27–256（230 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Chain B 260–432（173 aa） Fragment：UNP RESIDUES 27-256,UNP RESIDUES 2-161,UNP RESIDUES 260-432
Mutation：C54T, C97A Mutation：C54T, C97A 97V 4-{[(4-cyclohexylphenyl){[3-(methylsulfonyl)phenyl]carbamoyl}amino]methyl}-N-(1H-tetrazol-5-yl)benzamide × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100mM HEPES, pH7.0, 200mM potassium phospphate monobasic, 20% PEG500DME, 10 mM gly-gly-glysine
Resolution 3.19 Å R-free 0.231
5YQZ Structure of the glucagon receptor in complex with a glucagon analogue Deposited 2017-11-08 Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain R 27–257（231 aa）
Chain R 260–432（173 aa）
Mutation：R173A,C1053A, C1096Y Mutation：R173A,C1053A, C1096Y OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 6 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE；pH 8；293 K；100 mM Tris, pH 8.0, 70-120 mM potassium phosphate dibasic, 27-33% (v/v) PEG 200
Resolution 3.00 Å R-free 0.261
6LMK Cryo-EM structure of the human glucagon receptor in complex with Gs Deposited 2019-12-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–432（406 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.70 Å
6LML Cryo-EM structure of the human glucagon receptor in complex with Gi1 Deposited 2019-12-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–432（406 aa）
Mutation：E126R,T200W,A366M No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
6WHC CryoEM Structure of the glucagon receptor with a dual-agonist peptide Deposited 2020-04-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 1–477（477 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
6WPW GCGR-Gs signaling complex bound to a designed glucagon derivative Deposited 2020-04-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–477（451 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
7V35 Cryo-EM structure of the GIPR/GLP-1R/GCGR triagonist peptide 20-bound human GCGR-Gs complex Deposited 2021-08-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–432（406 aa）
Not recorded D6M N-hexadecanoyl-L-glutamic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8FU6 GCGR-Gs complex in the presence of RAMP2 Deposited 2023-01-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–477（451 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8JIQ Cryo-EM structure of the GLP-1R/GCGR dual agonist Peptide 15-bound human GCGR-Gs complex Deposited 2023-05-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–431（405 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8JIT Cryo-EM structure of the GLP-1R/GCGR dual agonist MEDI0382-bound human GCGR-Gs complex Deposited 2023-05-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–431（405 aa）
Not recorded D6M N-hexadecanoyl-L-glutamic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.91 Å
8JIU Cryo-EM structure of the GLP-1R/GCGR dual agonist SAR425899-bound human GCGR-Gs complex Deposited 2023-05-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–431（405 aa）
Not recorded D6M N-hexadecanoyl-L-glutamic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å
8JRU Cryo-EM structure of the glucagon receptor bound to beta-arrestin 1 in ligand-free state Deposited 2023-06-17 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain R 27–432（406 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
8JRV Cryo-EM structure of the glucagon receptor bound to glucagon and beta-arrestin 1 Deposited 2023-06-17 Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–432（406 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8WG8 Cryo-EM structures of peptide free and Gs-coupled GCGR Deposited 2023-09-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–432（407 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.71 Å
8YW5 Cryo-EM structure of the retatrutide-bound human GCGR-Gs complex Deposited 2024-03-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 27–432（406 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.84 Å
9MZG Cryo-EM structure of GCGR-Gs complex with glucagon Deposited 2025-01-22 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–477（452 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9N04 Cryo-EM structure of GCGR-Gs complex with peptide 15 Deposited 2025-01-23 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–477（452 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9N0E Cryo-EM structure of GCGR-Gs complex with oxyntomodulin Deposited 2025-01-24 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–477（452 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9N1Q cryo-EM structure of GCGR-Gs complex with SRB103H Deposited 2025-01-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–477（452 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9N2I cryo-EM structure of GCGR-Gs complex with SRB103Q Deposited 2025-01-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 26–477（452 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 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.