Current Protein Identity:O14842 New Search
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
4PHU Crystal structure of Human GPR40 bound to allosteric agonist TAK-875 Deposited 2014-05-07 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–211(211 aa) Fragment:UNP O14842 residues 2-213, UNP P00720 residues 2-161, UNP O14842 residues 214-300
Chain A 214–300(87 aa) Fragment:UNP O14842 residues 2-213, UNP P00720 residues 2-161, UNP O14842 residues 214-300
Mutation:L42A,F88A,G103A,Y202F,S211G,G212S,C1154T,C1197A Mutation:L42A,F88A,G103A,Y202F,S211G,G212S,C1154T,C1197A 2YB [(3S)-6-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy]biphenyl-3-yl}methoxy)-2,3-dihydro-1-benzofuran-3-yl]acetic acid × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 5 1PE PENTAETHYLENE GLYCOL × 1 DMS DIMETHYL SULFOXIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;pH 8;294 K;29-31% Peg 400,100 mM Tris pH 8.0. 0.2 M Na Malonate,200 uM TAK-875
X-ray crystallization conditions LIPIDIC CUBIC PHASE;pH 7.2;294 K;39.8 % Peg 400, 100 mM Bis-Tris-Propane pH 7.2, 0.1 Ammonium Phosphate (monobasic), 200 uM TAK-875
Resolution 2.33 Å R-free 0.233
5KW2 The extra-helical binding site of GPR40 and the structural basis for allosteric agonism and incretin stimulation Deposited 2016-07-15 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–211(211 aa)
Chain A 214–300(87 aa)
Not recorded 6XQ (3~{S})-3-cyclopropyl-3-[2-[1-[2-[2,2-dimethylpropyl-(6-methylpyridin-2-yl)carbamoyl]-5-methoxy-phenyl]piperidin-4-yl]-1-benzofuran-6-yl]propanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;298 K;0.1 M Tris HCl, pH 8.5, 30% PEG 400, 0.2 M ammonium formate.
Resolution 2.76 Å R-free 0.273
5TZR GPR40 in complex with partial agonist MK-8666 Deposited 2016-11-22 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–211(211 aa)
Chain A 214–300(87 aa)
Mutation:L42A, F88A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R Mutation:L42A, F88A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R NA SODIUM ION × 1 MK6 (5aR,6S,6aS)-3-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy][1,1'-biphenyl]-3-yl}methoxy)-5,5a,6,6a-tetrahydrocyclopropa[4,5]cyclopenta[1,2-c]pyridine-6-carboxylic acid × 1 MLI MALONATE ION × 1 OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 8 1PE PENTAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;pH 7.7;293 K;25-28%PEG 400, 0.2M sodium malonate, 0.1M Tris pH7.7
Resolution 2.20 Å R-free 0.228
5TZY GPR40 in complex with AgoPAM AP8 and partial agonist MK-8666 Deposited 2016-11-22 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–211(211 aa)
Chain A 214–300(87 aa)
Mutation:;L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R ; Mutation:;L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R,L42A, G103A, Y202F, R1012G, C1054T, C1097A, I1137R ; OLC (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate × 1 MK6 (5aR,6S,6aS)-3-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy][1,1'-biphenyl]-3-yl}methoxy)-5,5a,6,6a-tetrahydrocyclopropa[4,5]cyclopenta[1,2-c]pyridine-6-carboxylic acid × 1 7OS (2S,3R)-3-cyclopropyl-3-[(2R)-2-(1-{(1S)-1-[5-fluoro-2-(trifluoromethoxy)phenyl]ethyl}piperidin-4-yl)-3,4-dihydro-2H-1-benzopyran-7-yl]-2-methylpropanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions LIPIDIC CUBIC PHASE;pH 6.5;293 K;22% PEG 400, 0.37M potassium nitrate, 0.1M MES pH6.5
Resolution 3.22 Å R-free 0.287
8EIT Structure of FFAR1-Gq complex bound to DHA Deposited 2022-09-15 Assembly 1 Insufficient information Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain R 2–300(299 aa)
Not recorded HXA DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8EJC Structure of FFAR1-Gq complex bound to TAK-875 Deposited 2022-09-16 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain R 2–300(299 aa)
Not recorded 2YB [(3S)-6-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy]biphenyl-3-yl}methoxy)-2,3-dihydro-1-benzofuran-3-yl]acetic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8EJK Structure of FFAR1-Gq complex bound to TAK-875 in a lipid nanodisc Deposited 2022-09-17 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain R 2–300(299 aa)
Not recorded 2YB [(3S)-6-({2',6'-dimethyl-4'-[3-(methylsulfonyl)propoxy]biphenyl-3-yl}methoxy)-2,3-dihydro-1-benzofuran-3-yl]acetic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8T3V Cryo-EM structure of the DHA bound FFA1-Gq complex Deposited 2023-06-07 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain R 1–279(279 aa)
Not recorded CLR CHOLESTEROL × 1 HXA DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.39 Å
9K1C Cryo-EM structure of the DHA bound FFA1-Gi complex Deposited 2024-10-16 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain R 1–300(300 aa)
Not recorded HXA DOCOSA-4,7,10,13,16,19-HEXAENOIC ACID × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å