6phj

Crystal structure of native glucagon in space group P213 at 1.99 A resolution

Method: X-RAY DIFFRACTION D_max: 32.3 Å Quality: REASONABLE

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

Glucagon

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 53–81	Fragment：UNP residues 53-81	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1 M sodium/potassium tartrate, 0.2 M lithium sulfate, 0.1 M Tris, pH 7	Resolution 1.99 Å R-free 0.307

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 6PHJ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BH0 STRUCTURE OF A GLUCAGON ANALOG Deposited 1998-06-11	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 53–81（29 aa）	Mutation：R17K, R18K, D21E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions slow cooling of saturated soln；SLOW COOLING OF HEATED SUPERSATURATED SOLUTION, slow cooling of saturated soln	Resolution 3.00 Å
1D0R SOLUTION STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE IN TRIFLUOROETHANOL/WATER Deposited 1999-09-14	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 98–127（30 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 2.5；300 K；Pressure AMBIENT NMR sample composition 1.4MM GLUCAGON-LIKE PEPTIDE 1-(7-36)-AMIDE NMR sample composition 1.4MM GLUCAGON-LIKE PEPTIDE 1-(7-36)-AMIDE	Resolution not provided
1NAU NMR Solution Structure of the Glucagon Antagonist [desHis1, desPhe6, Glu9]Glucagon Amide in the Presence of Perdeuterated Dodecylphosphocholine Micelles Deposited 2002-11-28	Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa）	Mutation：DEL(H53), DEL(F58), D7E Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；310 K；Ionic strength (raw mmCIF value) 50 mM sodium phosphate; 1mM sodium azide；Pressure ambient NMR sample composition 7mM [desHis1, desPhe6, Glu9]Glucagon Amide; 50 mM sodium phosphate buffer; 283 mM dodecylphosphocholine-d38 micelles; 1 mM sodium azide; 90% H2O, 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2L63 NMR solution structure of GLP-2 in 2,2,2 trifluroethanol Deposited 2010-11-12	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–178（33 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；310 K；Pressure ambient NMR sample composition 33 % TFE-1, trifluoroethanol/water \| trifluoroethanol/water	Resolution not provided
2L64 NMR Solution structure of GLP-2 in DHPC micelles Deposited 2010-11-12	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 146–178（33 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 3.9；310 K；Pressure ambient NMR sample composition 350 mM DHPC-1, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2M5P Solution structure of lipidated glucagon analog in water Deposited 2013-03-03	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 53–81（29 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	GGL GAMMA-L-GLUTAMIC ACID × 2 PLM PALMITIC ACID × 1	SOLUTION NMR NMR measurement conditions pH 4.7；298 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient NMR sample composition 0.7 mM peptide, 20 mM sodium phosphate, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2M5Q Solution structure of lipidated glucagon analog in d-TFE Deposited 2013-03-04	Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain X 53–81（29 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	GGL GAMMA-L-GLUTAMIC ACID × 2 PLM PALMITIC ACID × 1	SOLUTION NMR NMR measurement conditions pH 5；298 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR sample composition 0.7 mM protein, 95% [U-100% 2H] TFE/5% H2O \| 95% [U-100% 2H] TFE/5% H2O	Resolution not provided
3IOL Crystal structure of Glucagon-Like Peptide-1 in complex with the extracellular domain of the Glucagon-Like Peptide-1 Receptor Deposited 2009-08-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 98–128（31 aa） Fragment：UNP residues 98-128	Not recorded	10M decyl 4-O-alpha-D-glucopyranosyl-1-thio-beta-D-glucopyranoside × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.9；291 K；0.1M N-(2-Acetamido) Iminodiacetic Acid (ADA), pH 6.9, 14 vol-% (+/-)-2-Methyl-2,4-pentanediol (MPD), 9mM n-decyl-beta-D-thiomaltoside, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 2.10 Å R-free 0.226
4APD Liraglutide Deposited 2012-04-02	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 98–128（31 aa）	Not recorded	D6M N-hexadecanoyl-L-glutamic acid × 1	SOLUTION NMR NMR measurement conditions pH 7.9；300 K；Pressure 1.0 NMR sample composition 10% D2O / 90% H2O	Resolution not provided
5OTU Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Hcs Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 98–128（31 aa）	Mutation：A8HCS, T11HCS Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution G1: 0.1 M Carboxylic acids, 0.1 Buffer system 1 pH 6.5, 20% (v/v) PEG500mme, 10% (w/v) PEG20000	Resolution 1.80 Å R-free 0.211
5OTU Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Hcs Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 98–128（31 aa）	Mutation：A8HCS, T11HCS Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution G1: 0.1 M Carboxylic acids, 0.1 Buffer system 1 pH 6.5, 20% (v/v) PEG500mme, 10% (w/v) PEG20000	Resolution 1.80 Å R-free 0.211
5OTV Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cyc/Thr11Hcs Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 98–128（31 aa）	Mutation：A8C, T11HCS Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000	Resolution 2.00 Å R-free 0.246
5OTV Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cyc/Thr11Hcs Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 98–128（31 aa）	Mutation：A8C, T11HCS Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution E5: 0.12 M Ethylene Glycols, 0.1 M Buffer System 2 pH 7.5, 205 (v/v) PEg500mme, 10% (w/v) PEG20000	Resolution 2.00 Å R-free 0.246
5OTW Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Cys Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 98–128（31 aa）	Mutation：A8HCS, T11C Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution E12: 0.12 M ethylene Glycols, 0.1 M Buffer system 3 pH 8.5, 12.5% (v/v) MPD, 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350	Resolution 2.10 Å R-free 0.239
5OTW Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Hcs/Thr11Cys Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 98–128（31 aa）	Mutation：A8HCS, T11C Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions, solution E12: 0.12 M ethylene Glycols, 0.1 M Buffer system 3 pH 8.5, 12.5% (v/v) MPD, 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350	Resolution 2.10 Å R-free 0.239
5OTX Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cys/Thr11Cys Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 98–128（31 aa）	Mutation：A8C, T11C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions solution F2: 0.12 M Monosaccharides, 0.1 M Buffer system 1 pH 6.5, 20% (v/v) Ethylene Glycol, 10% (w/v) PEG8000	Resolution 2.00 Å R-free 0.240
5OTX Extracellular domain of GLP-1 receptor in complex with GLP-1 variant Ala8Cys/Thr11Cys Deposited 2017-08-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 98–128（31 aa）	Mutation：A8C, T11C	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Morpheus from Molecular Dimensions solution F2: 0.12 M Monosaccharides, 0.1 M Buffer system 1 pH 6.5, 20% (v/v) Ethylene Glycol, 10% (w/v) PEG8000	Resolution 2.00 Å R-free 0.240
5VAI Cryo-EM structure of the activated Glucagon-like peptide-1 receptor in complex with G protein Deposited 2017-03-27	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–128（31 aa） Fragment：UNP residues 98-128	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.10 Å
6EDS Structure of Cysteine-free Human Insulin-Degrading Enzyme in complex with Glucagon and Substrate-selective Macrocyclic Inhibitor 63 Deposited 2018-08-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 53–81（29 aa）	Not recorded	J22 {(8R,9S,10S)-9-(2',3'-dimethyl[1,1'-biphenyl]-4-yl)-6-[(1-methyl-1H-imidazol-2-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]decan-10-yl}methanol × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1M HEPES pH 7.0, 12% Tacsimate pH 7.0, 13% PEGMME, 10% Dioxane	Resolution 3.18 Å R-free 0.222
6EDS Structure of Cysteine-free Human Insulin-Degrading Enzyme in complex with Glucagon and Substrate-selective Macrocyclic Inhibitor 63 Deposited 2018-08-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 53–81（29 aa）	Not recorded	J22 {(8R,9S,10S)-9-(2',3'-dimethyl[1,1'-biphenyl]-4-yl)-6-[(1-methyl-1H-imidazol-2-yl)sulfonyl]-1,6-diazabicyclo[6.2.0]decan-10-yl}methanol × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1 DIO 1,4-DIETHYLENE DIOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1M HEPES pH 7.0, 12% Tacsimate pH 7.0, 13% PEGMME, 10% Dioxane	Resolution 3.18 Å R-free 0.222
6LMK Cryo-EM structure of the human glucagon receptor in complex with Gs Deposited 2019-12-26	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 53–81（29 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	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain E 53–81（29 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6NZN Dimer-of-dimer amyloid fibril structure of glucagon Deposited 2019-02-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 53–81（29 aa） Chain B 53–81（29 aa） Chain C 53–81（29 aa） Chain D 53–81（29 aa） Chain E 53–81（29 aa） Chain F 53–81（29 aa） Chain G 53–81（29 aa） Chain H 53–81（29 aa） Chain I 53–81（29 aa） Chain J 53–81（29 aa） Chain K 53–81（29 aa） Chain L 53–81（29 aa） Chain M 53–81（29 aa） Chain N 53–81（29 aa） Chain O 53–81（29 aa） Chain P 53–81（29 aa）	Not recorded	No recorded non-water small molecule	SOLID-STATE NMR NMR measurement conditions pH 2；293 K；Ionic strength (raw mmCIF value) 0.01；Pressure 1 NMR sample composition 0.1 mg/uL {U-13C; U-15N]-G4,S8,L14,A19,V23 Glucagon, water \| water NMR sample composition 0.1 mg/uL {U-13C; U-15N]-S2,Q3,G4,T5,Q24,W25,L26,M27,N28 Glucagon, water \| water NMR sample composition 0.1 mg/uL {U-13C; U-15N]-T5,F6,T7,S8,D9,Y10,S11,A19,Q20,D21,F22,V23,Q24 Glucagon, water \| water NMR sample composition 0.1 mg/uL {U-13C; U-15N]-S11,K12,Y13,L14,D15,S16,R17,R18,A19 Glucagon, water \| water	Resolution not provided
6PHI Crystal structure of native glucagon in space group I41 at 1.1 A resolution Deposited 2019-06-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa） Fragment：UNP residues 53-81	Not recorded	CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；2.5 M sodium chloride, 0.1 M imidazole, pH 8	Resolution 1.10 Å R-free 0.139
6PHK Crystal structure of glucagon analog with mono-stereoinversion at position 21 (D-Asp21) in space group I41 at 1.18 A resolution Deposited 2019-06-25	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa） Fragment：UNP residues 53-81	Mutation：D21D-Asp Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293 K；0.2 M lithium sulfate, 20% butanediol, 0.1 M MES, pH 6	Resolution 1.18 Å R-free 0.162
6PHL Crystal structure of glucagon analog with mono-stereoinversion at position 23 (D-Val23) in space group I41 at 1.44 A resolution Deposited 2019-06-25	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa） Fragment：UNP residues 53-81	Mutation：V23D-Val Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；tri-sodium citrate, pH 5.5, 20% PEG3000	Resolution 1.44 Å R-free 0.169
6PHO Crystal structure of glucagon analog with selenomethionine substitutions at position 1 and 27 in space group I41 at 1.42 A resolution Deposited 2019-06-25	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa） Fragment：UNP residues 53-81	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.2 M tri-potassium citrate, 20% PEG3350	Resolution 1.42 Å R-free 0.189
6PHP Crystal structure of glucagon analog with 4-bromo-phenylalanine substitutions at position 6 and 22 in space group I41 at 1.65 A resolution Deposited 2019-06-25	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 53–81（29 aa） Fragment：UNP residues 53-81	Mutation：F6BrF, F22BrF Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Tacsimate, pH 4, 16% PEG3350, 0.1 M sodium acetate, pH 4.6	Resolution 1.65 Å R-free 0.246
6VCB Cryo-EM structure of the Glucagon-like peptide-1 receptor in complex with G protein, GLP-1 peptide and a positive allosteric modulator Deposited 2019-12-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–128（31 aa）	Not recorded	QW7 1-[(1R)-1-(2,6-dichloro-3-methoxyphenyl)ethyl]-6-{2-[(2R)-piperidin-2-yl]phenyl}-1H-benzimidazole × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
6X18 GLP-1 peptide hormone bound to Glucagon-Like peptide-1 (GLP-1) Receptor Deposited 2020-05-18	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–127（30 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.10 Å
7D68 Cryo-EM structure of the human glucagon-like peptide-2 receptor-Gs protein complex Deposited 2020-09-29	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 146–178（33 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
7DUQ Cryo-EM structure of the compound 2 and GLP-1-bound human GLP-1 receptor-Gs complex Deposited 2021-01-11	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–127（30 aa）	Not recorded	HNO N-tert-butyl-6,7-bis(chloranyl)quinoxalin-2-amine × 1 CLR CHOLESTEROL × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.50 Å
7XM8 Glucagon amyloid fibril Deposited 2022-04-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 22 PDB declaration: 22-meric	Chain A 53–81（29 aa） Chain B 53–81（29 aa） Chain C 53–81（29 aa） Chain D 53–81（29 aa） Chain E 53–81（29 aa） Chain F 53–81（29 aa） Chain G 53–81（29 aa） Chain H 53–81（29 aa） Chain I 53–81（29 aa） Chain J 53–81（29 aa） Chain K 53–81（29 aa） Chain L 53–81（29 aa） Chain M 53–81（29 aa） Chain N 53–81（29 aa） Chain O 53–81（29 aa） Chain P 53–81（29 aa） Chain Q 53–81（29 aa） Chain R 53–81（29 aa） Chain S 53–81（29 aa） Chain T 53–81（29 aa） Chain U 53–81（29 aa） Chain V 53–81（29 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 2.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
8JRV Cryo-EM structure of the glucagon receptor bound to glucagon and beta-arrestin 1 Deposited 2023-06-17	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain G 53–81（29 aa）	Not recorded	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
9E2A Glucagon Like Peptide Receptor-1 (GLP1R) A316T mutant with GLP-1 peptide. Dominant negative Gs complex. Deposited 2024-10-22	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–127（30 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9N0E Cryo-EM structure of GCGR-Gs complex with oxyntomodulin Deposited 2025-01-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 53–89（37 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
9X20 Cryo-EM structure of the GLP-1-bound human GLP-1R-Gi complex Deposited 2025-10-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 98–127（30 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å
9X22 Cryo-EM structure of the GLP-1-bound human GLP-1R-Gq complex Deposited 2025-10-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain P 98–127（30 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.92 Å

33 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	GLUC_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–29； UniProt 53–81

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6phj
Deposition date deposition_date	2019-06-25
Structure title title	Crystal structure of native glucagon in space group P213 at 1.99 A resolution
Keywords keywords	glucagon, GPCR ligand, peptide hormone, HORMONE; HORMONE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	11.65 Å
Radius of gyration Rg (electron density) rg_electron	11.40 Å
Forward intensity I(0) i0	259459.00
Molecular weight molecular_weight	3012.0 kDa
Excluded volume excluded_volume	3721 Å³
Envelope volume envelope_volume	4459 Å³
Hydration-shell volume shell_volume	4236 Å³
Envelope diameter envelope_diameter	42.1 Å
Shell Rg shell_rg	14.53 Å
Envelope Rg envelope_rg	12.03 Å
Shape Rg shape_rg	11.38 Å
Total Rg total_rg	12.47 Å
Total atoms total_atoms	406
Residues n_residues	25
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	32.3 Å
Rg (real space) rg_real	10.98 Å
Rg uncertainty (real space) rg_real_error	0.07 Å
I(0) (real space) i0_real	2.4930e+05
I(0) uncertainty (real space) i0_real_error	2.1220e+03
Rg (reciprocal space) rg_reciprocal	11.93 Å
I(0) (reciprocal space) i0_reciprocal	259500.0000
Solution quality estimate total_estimate	0.6569
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	0
Primary peak position r_peak_primary	— Å
Skewness Skewness skewness	0.408
Kurtosis Kurtosis kurtosis	-0.610
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	4.2730
Highest regularization parameter α highest_alpha	11420.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.982; Stabil: 0.966; Sysdev: 0.000; Positv: 1.000; Valcen: 0.701; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (2)

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Unit-cell length a length_a	44.724 Å
Unit-cell length b length_b	44.724 Å
Unit-cell length c length_c	44.724 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	12

Space group space_group	P 21 3
Space-group number int_tables_number	198
Crystal system crystal_system	—

Resolution resolution	1.990 Å
Low-resolution limit resolution_low	31.625 Å
R factor r_factor	0.2812
R_work r_work	0.2797
R_free r_free	0.3075

Description description	Glucagon
Molecular weight formula_weight	3486.8 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	433

Crystal structure of native glucagon in space group P213 at 1.99 A resolution

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

Glucagon

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

8. Citations (2)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	2

fit	/app/data/saxs_computation/ph/6phj/6phj.fit
pddf	/app/data/pr_computation/ph/6phj/6phj.pr.out
profile	/app/data/saxs_computation/ph/6phj/6phj.dat