SAXSdb — 8j8r

▼

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

Beta-arrestin-2

Bos taurus

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain A； UniProt 1–420 Chain B； UniProt 1–420 Chain C； UniProt 1–420	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	Fab30 Heavy Chain × 3 Fab30 Light Chain × 3 Muscarinic acetylcholine receptor M2 × 3 （P08172）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.90 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 8J8R	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5TV1 active arrestin-3 with inositol hexakisphosphate Deposited 2016-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 8–393（386 aa） Fragment：UNP residues 8-393	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 6 GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；100 mM Succinate/Phosphate/Glycine pH 8.5 and 25% PEG 1500	Resolution 2.40 Å R-free 0.245
8GO9 Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Atypical chemokine receptor 2, ACKR2 (D6R) Deposited 2022-08-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–420（420 aa） Chain F 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.35 Å
8GOC Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R Deposited 2022-08-24	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.18 Å
8GOO Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human C5a anaphylatoxin chemotactic receptor 1, C5aR1 Deposited 2022-08-25	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.40 Å
8I0Z Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human C5a anaphylatoxin chemotactic receptor 1, C5aR1 (Local refine) Deposited 2023-01-12	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.33 Å
8I10 Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R (Local refine) Deposited 2023-01-12	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.96 Å
8J8V Structure of beta-arrestin2 in complex with D6Rpp (Local Refine) Deposited 2023-05-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–420（420 aa） Chain F 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.22 Å
8TIL Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 reconstructed without receptor/micelle Deposited 2023-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8TIN Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 reconstructed without receptor/micelle Deposited 2023-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
8VJ9 CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted Deposited 2024-01-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa） Fragment：Arrestin3 variant with the C edge loop from Arrestin2 inserted	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
9KY2 Structure of beta-arrestin2 in complex with mouse C5aR1pp Deposited 2024-12-07	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–420（420 aa） Chain F 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.78 Å

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ARRB2_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–420； UniProt 1–420 Author chain B； PDBConstruct 1–420； UniProt 1–420 Author chain C； PDBConstruct 1–420； UniProt 1–420

Muscarinic acetylcholine receptor M2

OrganismNot specified

UniProt P08172

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count	Chain G； UniProt 300–317 Chain U； UniProt 300–317 Chain V； UniProt 300–317	Fragment：ICL3 Non-standard monomer：Yes (specific site not provided by mmCIF)	Beta-arrestin-2 × 3 （P32120） Fab30 Heavy Chain × 3 Fab30 Light Chain × 3	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.90 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 8J8R	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3UON Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist Deposited 2011-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–217（217 aa） Fragment：UNP RESIDUES 1-217, UNP RESIDUES 2-161, UNP RESIDUES 377-466 Chain A 377–466（90 aa） Fragment：UNP RESIDUES 1-217, UNP RESIDUES 2-161, UNP RESIDUES 377-466	Mutation：N2D, N3D, N6D, N9D, C54T, C97A Mutation：N2D, N3D, N6D, N9D, C54T, C97A	QNB (3R)-1-azabicyclo[2.2.2]oct-3-yl hydroxy(diphenyl)acetate × 1 BGC beta-D-glucopyranose × 1 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.5；293 K；25 to 35% PEG 300, 100 mM ammonium phosphate, 2% 2-Methyl-2,4-pentanediol, 100 mM HEPES, 10:1 monoolein:cholesterol lipid mix diluted 1.5:1 with protein in detergent buffer, Lipidic cubic phase, temperature 293K, pH 7.5	Resolution 3.00 Å R-free 0.276
4MQS Structure of active human M2 muscarinic acetylcholine receptor bound to the agonist iperoxo Deposited 2013-09-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–232（232 aa） Fragment：UNP residues 1-232, 373-466 Chain A 373–466（94 aa） Fragment：UNP residues 1-232, 373-466	Mutation：N0D, N1D, N4D, N7D, A373T, K374R Mutation：N0D, N1D, N4D, N7D, A373T, K374R	IXO 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；Reconstituted in 10:1 monoolein:cholesterol mix. Precipitant solution: 10 - 20% PEG300, 100 mM HEPES, pH 7.2 - 7.9, 1.2% 1,2,3-heptanetriol, and 20 - 80 mM EDTA, pH 8.0, Lipidic cubic phase, temperature 293K	Resolution 3.50 Å R-free 0.298
4MQT Structure of active human M2 muscarinic acetylcholine receptor bound to the agonist iperoxo and allosteric modulator LY2119620 Deposited 2013-09-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–232（232 aa） Fragment：UNP residues 1-232,373-466 Chain A 373–466（94 aa） Fragment：UNP residues 1-232,373-466	Mutation：N0D, N1D, N4D, N7D, A373T, K374R Mutation：N0D, N1D, N4D, N7D, A373T, K374R	IXO 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium × 1 2CU 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；Reconstituted in 10:1 monoolein:cholesterol mix. Precipitant solution: 0.5 mM LY2119620, 10 - 20% PEG300, 100 mM HEPES pH 7.2 - 7.9, 1.2% 1,2,3-heptanetriol, and 20 - 80 mM EDTA pH 8.0, Lipidic cubic phase, temperature 293K	Resolution 3.70 Å R-free 0.301
5YC8 Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with NMS (Hg-derivative) Deposited 2017-09-06	Different construct Different mutation/modification Different oligomeric state 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 10–214（205 aa） Fragment：UNP residues 10-214,UNP residues 377-466 Chain A 377–466（90 aa） Fragment：UNP residues 10-214,UNP residues 377-466	Mutation：S110R Mutation：S110R	3C0 N-methyl scopolamine × 1 HG MERCURY (II) ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；50mM MES-NaOH pH 6.2-7.0, 26-32% PEG300, 300~500mM Ammonium Fluoride, 1% 1,2,3-heptanetriol, 0.5mM NMS and 5% DMSO, 1mM HgCl2	Resolution 2.50 Å R-free 0.270
5ZK3 Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with QNB Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state 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 10–217（208 aa） Fragment：UNP residues 10-217,UNP residues 377-466 Chain A 377–466（90 aa） Fragment：UNP residues 10-217,UNP residues 377-466	Mutation：S110R Mutation：S110R	QNB (3R)-1-azabicyclo[2.2.2]oct-3-yl hydroxy(diphenyl)acetate × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；50mM MES-NaOH pH 6.2-7.0, 26-32% PEG300, 300~500mM Ammonium Fluoride, 1% 1,2,3-heptanetriol, 0.5mM QNB and 5% DMSO	Resolution 2.60 Å R-free 0.291
5ZK8 Crystal structure of M2 muscarinic acetylcholine receptor bound with NMS Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state 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 10–217（208 aa） Fragment：UNP residues 10-217,UNP residues 377-466 Chain A 377–466（90 aa） Fragment：UNP residues 10-217,UNP residues 377-466	Not recorded	3C0 N-methyl scopolamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；50mM MES-NaOH pH 6.2-7.0, 26-32 % PEG300, 300~500mM Ammonium Fluoride, 1% 1,2,3-heptanetriol, 0.5mM NMS and 5% DMSO	Resolution 3.00 Å R-free 0.270
5ZKB Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with AF-DX 384 Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state 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 10–217（208 aa） Fragment：UNP residues 10-217,UNP residues 377-466 Chain A 377–466（90 aa） Fragment：UNP residues 10-217,UNP residues 377-466	Mutation：S110R Mutation：S110R	82F N-[2-[(2S)-2-[(dipropylamino)methyl]piperidin-1-yl]ethyl]-6-oxidanylidene-5H-pyrido[2,3-b][1,4]benzodiazepine-11-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；50mM MES-NaOH pH 6.2-7.0, 18 % PEG300, 100mM Magnesium acetate, 1% 1,2,3-heptanetriol, 0.5mM AF-DX 384 and 5% DMSO	Resolution 2.95 Å R-free 0.280
5ZKC Crystal structure of rationally thermostabilized M2 muscarinic acetylcholine receptor bound with NMS Deposited 2018-03-23	Different construct Different mutation/modification Different oligomeric state 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 10–217（208 aa） Fragment：UNP residues 10-217,UNP residues 377-466 Chain A 377–466（90 aa） Fragment：UNP residues 10-217,UNP residues 377-466	Mutation：S110R Mutation：S110R	3C0 N-methyl scopolamine × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；50mM MES-NaOH pH 6.2-7.0, 26-32 % PEG300, 300~500mM Ammonium Fluoride, 1% 1,2,3-heptanetriol, 0.5mM NMS and 5% DMSO	Resolution 2.30 Å R-free 0.259
6OIK Muscarinic acetylcholine receptor 2-Go complex Deposited 2019-04-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 3–232（230 aa） Chain R 360–466（107 aa）	Mutation：N8A, N11D, N14D,N11D, N14D Mutation：N8A, N11D, N14D,N11D, N14D	IXO 4-(4,5-dihydro-1,2-oxazol-3-yloxy)-N,N,N-trimethylbut-2-yn-1-aminium × 1 2CU 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
6U1N GPCR-Beta arrestin structure in lipid bilayer Deposited 2019-08-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain R 2–466（465 aa） Fragment：M2 UNP residues 2-466 + V2 UNP residues 343-371	Non-standard monomer：Yes (specific site not provided by mmCIF)	2CU 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
7T8X Cryo-EM structure of ACh-bound M2R-Go signaling complex in S1 state Deposited 2021-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 4–232（229 aa） Chain A 368–466（99 aa）	Not recorded	ACH ACETYLCHOLINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.21 Å
7T90 Cryo-EM structure of ACh-bound M2R-Go signaling complex in S2 state Deposited 2021-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 4–232（229 aa） Chain A 368–466（99 aa）	Not recorded	ACH ACETYLCHOLINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.32 Å
7T94 Cryo-EM structure of S1 state ACh-bound M2R-Go signaling complex with a PAM Deposited 2021-12-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 4–232（229 aa） Chain A 368–466（99 aa）	Not recorded	ACH ACETYLCHOLINE × 1 2CU 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.16 Å
7T96 Cryo-EM structure of S2 state ACh-bound M2R-Go signaling complex with a PAM Deposited 2021-12-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 4–232（229 aa） Chain A 368–466（99 aa）	Not recorded	ACH ACETYLCHOLINE × 1 2CU 3-amino-5-chloro-N-cyclopropyl-4-methyl-6-[2-(4-methylpiperazin-1-yl)-2-oxoethoxy]thieno[2,3-b]pyridine-2-carboxamide × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.22 Å
8J97 Structure of Muscarinic receptor (M2R) in complex with beta-arrestin1 (Local refine, cross-linked) Deposited 2023-05-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain V 305–313（9 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8JAF Structure of Muscarinic receptor (M2R) in complex with beta-arrestin1 (Local Refine, non-cross linked) Deposited 2023-05-05	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain V 307–313（7 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ACM2_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain G； PDBConstruct 1–18； UniProt 300–317 Author chain U； PDBConstruct 1–18； UniProt 300–317 Author chain V； PDBConstruct 1–18； UniProt 300–317

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	8j8r
Deposition date deposition_date	2023-05-02
Structure title title	Structure of beta-arrestin2 in complex with M2Rpp
Keywords keywords	GPCR, Arrestin, SIGNALING PROTEIN, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	44.54 Å
Radius of gyration Rg (electron density) rg_electron	43.95 Å
Forward intensity I(0) i0	528885000.00
Molecular weight molecular_weight	190190.0 kDa
Excluded volume excluded_volume	238580 Å³
Envelope volume envelope_volume	343800 Å³
Hydration-shell volume shell_volume	65420 Å³
Envelope diameter envelope_diameter	138.7 Å
Shell Rg shell_rg	49.19 Å
Envelope Rg envelope_rg	42.55 Å
Shape Rg shape_rg	43.93 Å
Total Rg total_rg	44.27 Å
Total atoms total_atoms	13424
Residues n_residues	1724
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

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	140.2 Å
Rg (real space) rg_real	44.40 Å
Rg uncertainty (real space) rg_real_error	1.06 Å
I(0) (real space) i0_real	5.2890e+08
I(0) uncertainty (real space) i0_real_error	8.5340e+06
Rg (reciprocal space) rg_reciprocal	44.54 Å
I(0) (reciprocal space) i0_reciprocal	529000000.0000
Solution quality estimate total_estimate	0.9036
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	52.1 Å
Skewness Skewness skewness	0.143
Kurtosis Kurtosis kurtosis	-0.690
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	42670000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.858

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Beta-arrestin-2
Molecular weight formula_weight	47217.7 kDa
Mutation mutation	C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	13424

MGEKPGTRVFKKSSPNGKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTVAFRYGREDCDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPSSVTLQPGPEDTGKALGVDFEIRAFVAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADIVLFSTAQYKVPVAQVEQDDQVSPSSTFSKVYTITPFLANNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC

来源 Source

来源生物 organism	Bos taurus
通用名 common_name	cattle
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Fab30 Heavy Chain
Molecular weight formula_weight	25512.4 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,H,M

EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGYTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH

来源 Source

来源生物 organism	Mus musculus
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Fab30 Light Chain
Molecular weight formula_weight	23435.1 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,L,N

SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

来源 Source

来源生物 organism	Mus musculus
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Muscarinic acetylcholine receptor M2
Molecular weight formula_weight	2362.9 kDa
Source method src_method	syn
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,U,V

EITQDENTVSTSLGHSKD

▶

8. Citations (1)

▶

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	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	triclinic

Resolution resolution	2.90 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	224494

fit	/app/data/saxs_computation/j8/8j8r/8j8r.fit
pddf	/app/data/pr_computation/j8/8j8r/8j8r.pr.out
profile	/app/data/saxs_computation/j8/8j8r/8j8r.dat

Structure of beta-arrestin2 in complex with M2Rpp

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

Beta-arrestin-2

State in the Current Structure

Other States of the Same Protein in the Database

Muscarinic acetylcholine receptor M2

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)