SAXSdb — 9uco

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

Beta-arrestin-1

Mus musculus

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 1–376 Chain C； UniProt 1–376	Not recorded	scFv30 × 4 Adhesion G protein-coupled receptor E1 × 2 （Q61549） Adhesion G protein-coupled receptor E1 × 2 （Q61549）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.58 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 9UCO	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1G4M CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1 Deposited 2000-10-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–393（393 aa） Fragment：TRUNCATION MUTANT: 1-393	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.269
1G4M CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1 Deposited 2000-10-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–393（393 aa） Fragment：TRUNCATION MUTANT: 1-393	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å R-free 0.269
1G4R CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1 Deposited 2000-10-27	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–393（393 aa） Fragment：TRUNCATION MUTANT: 1-393	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.274
1JSY Crystal structure of bovine arrestin-2 Deposited 2001-08-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–418（418 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；magnesium formate, polypropylene glycol 400, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.238
1ZSH Crystal structure of bovine arrestin-2 in complex with inositol hexakisphosphate (IP6) Deposited 2005-05-24	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 1–418（418 aa）	Not recorded	MG MAGNESIUM ION × 1 IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.2；298 K；Magnesium Formate, HEPES, Polypropylene glycol 400, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.90 Å R-free 0.260
2WTR Full length Arrestin2 Deposited 2009-09-21	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 1–418（418 aa）	Not recorded	BA BARIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；CRYSTALS WERE GROWN USING THE HANGING-DROP METHOD IN A NEXTAL TRAY (QIAGEN) AT 277 K AGAINST A 1 ML RESERVOIR SOLUTION CONSISTING OF 12% (W/V) PEG 2000, 0.1M BACL2, 0.1 M TRIS-HCL PH7.5. THE HANGING DROP CONTAINED 2 MICROLITRES OF CONCENTRATED ARRESTIN2 PROTEIN (BETWEEN 9-11 MG/ML IN 0.1M TRIS-HCL PH 8.5) AND 2 MICROLITRES OF RESERVOIR SOLUTION.	Resolution 2.90 Å R-free 0.295
2WTR Full length Arrestin2 Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 1–418（418 aa）	Not recorded	BA BARIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；CRYSTALS WERE GROWN USING THE HANGING-DROP METHOD IN A NEXTAL TRAY (QIAGEN) AT 277 K AGAINST A 1 ML RESERVOIR SOLUTION CONSISTING OF 12% (W/V) PEG 2000, 0.1M BACL2, 0.1 M TRIS-HCL PH7.5. THE HANGING DROP CONTAINED 2 MICROLITRES OF CONCENTRATED ARRESTIN2 PROTEIN (BETWEEN 9-11 MG/ML IN 0.1M TRIS-HCL PH 8.5) AND 2 MICROLITRES OF RESERVOIR SOLUTION.	Resolution 2.90 Å R-free 0.295
3GC3 Crystal Structure of Arrestin2S and Clathrin Deposited 2009-02-21	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–385（385 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM bis_tris propane 4 -4.5 M ammonium acetate 4.5% ethylene glycol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.20 Å R-free 0.251
3GD1 Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking Deposited 2009-02-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 1–393（393 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；293 K；100mM Bicine, 7% O-(2-aminopropyl)-O'-(2-methoxyethyl)polypropylene glycol 500, 6% polyethylene glycol 8000, 4% acetone, 1% ethylene glycol and 10 mM strontium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.254
3GD1 Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking Deposited 2009-02-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain E 1–393（393 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；293 K；100mM Bicine, 7% O-(2-aminopropyl)-O'-(2-methoxyethyl)polypropylene glycol 500, 6% polyethylene glycol 8000, 4% acetone, 1% ethylene glycol and 10 mM strontium chloride, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.50 Å R-free 0.254
6NI2 Stabilized beta-arrestin 1-V2T subcomplex of a GPCR-G protein-beta-arrestin mega-complex Deposited 2018-12-26	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain B 1–393（393 aa） Fragment：UNP residues 6-361	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
7DF9 Crystal of Arrestin2-V2Rpp-1-Fab30 complex Deposited 2020-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–418（418 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；10% PEG 3350, 0.1M Succinic acid, pH 6.5-7.5, 0.2mM DMSO	Resolution 3.17 Å R-free 0.281
7DFA Crystal of Arrestin2-V2Rpp-4-Fab30 complex Deposited 2020-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–418（418 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；10% PEG 3350, 0.1M Succinic acid, pH 6.5-7.5, 0.2mM DMSO	Resolution 2.54 Å R-free 0.280
7DFB Crystal of Arrestin2-V2Rpp-6-7-Fab30 complex Deposited 2020-11-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–418（418 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；289 K；0% PEG 3350, 0.1M Succinic acid, pH 6.5-7.5, 0.2mM DMSO	Resolution 3.28 Å R-free 0.290
7DFC Crystal of Arrestin2-V2Rpp-3-Fab30 complex Deposited 2020-11-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–418（418 aa）	Not recorded	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 7.5；289 K；15% PEG 3350, 0.1M HEPES, 0.2mM DMSO	Resolution 2.49 Å R-free 0.284
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 A 5–357（353 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 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 A 5–362（358 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8TII Human ACKR3 phosphorylated by GRK2 in complex with Arrestin2 in nanodisc 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 × 5 PDB declaration: pentameric	Chain A 1–418（418 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
8TIO Human ACKR3 with C tail extended by 12 glycines phosphorylated by GRK5 in complex with Arrestin2 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 1–418（418 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
8WU1 Cryo-EM structure of CB1-beta-arrestin1 complex Deposited 2023-10-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 1–393（393 aa）	Mutation：R169E, I386A, V387A, F388A	KCA methyl N-{1-[(4-fluorophenyl)methyl]-1H-indazole-3-carbonyl}-3-methyl-L-valinate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9E82 ACKR3 phosphorylated by GRK5 in complex with arrestin2 and Fab7 Deposited 2024-11-04	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 1–418（418 aa）	Not recorded	CLR CHOLESTEROL × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
9LZ0 Cryo-EM structure of PTH1R-beta-arrestin1 complex in state 1 Deposited 2025-02-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–393（393 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
9LZ1 Cryo-EM structure of PTH1R-beta-arrestin1 complex in state 2 Deposited 2025-02-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–393（393 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
9LZ2 Cryo-EM structure of PTH1R(V2RC)-beta-arrestin1 complex Deposited 2025-02-21	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain A 1–393（393 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
9WSV Cryo-EM structure of DAMGO-muOR-arrestin-1-Fab30 complex Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–393（393 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
9WSX Cryo-EM structure of endomorphin-1-muOR-arrestin2-Fab30 complex Deposited 2025-09-15	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 1–393（393 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å

23 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ARRB1_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–376； UniProt 1–376 Author chain C； PDBConstruct 1–376； UniProt 1–376

Adhesion G protein-coupled receptor E1

Mus musculus

UniProt Q61549

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 × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain G； UniProt 630–644 Chain H； UniProt 645–931 Chain L； UniProt 630–644 Chain R； UniProt 645–931	Not recorded	Beta-arrestin-1 × 2 （P17870） scFv30 × 4	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.58 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	AGRE1_MOUSE
Isoform	—
PDB entities	3, 4
Chains and sequence ranges	Author chain G； PDBConstruct 1–15； UniProt 630–644 Author chain L； PDBConstruct 1–15； UniProt 630–644 Author chain H； PDBConstruct 1–287； UniProt 645–931 Author chain R； PDBConstruct 1–287； UniProt 645–931

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9uco
Deposition date deposition_date	2025-04-04
Structure title title	Cryo-EM structure of ADGRE1-beta arrestin1-scFv30 complex
Keywords keywords	complex, membrane protein, ADGRE1; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	46.81 Å
Radius of gyration Rg (electron density) rg_electron	46.38 Å
Forward intensity I(0) i0	394667000.00
Molecular weight molecular_weight	171850.0 kDa
Excluded volume excluded_volume	218250 Å³
Envelope volume envelope_volume	322470 Å³
Hydration-shell volume shell_volume	59253 Å³
Envelope diameter envelope_diameter	169.7 Å
Shell Rg shell_rg	49.73 Å
Envelope Rg envelope_rg	44.80 Å
Shape Rg shape_rg	46.37 Å
Total Rg total_rg	46.58 Å
Total atoms total_atoms	12144
Residues n_residues	1653
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	158.5 Å
Rg (real space) rg_real	46.74 Å
Rg uncertainty (real space) rg_real_error	1.94 Å
I(0) (real space) i0_real	3.9470e+08
I(0) uncertainty (real space) i0_real_error	9.0570e+06
Rg (reciprocal space) rg_reciprocal	46.81 Å
I(0) (reciprocal space) i0_reciprocal	394700000.0000
Solution quality estimate total_estimate	0.8169
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	55.9 Å
Skewness Skewness skewness	0.176
Kurtosis Kurtosis kurtosis	-0.492
Angular range angular_range	— – 0.1700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	23240000.0000
Real-space data points n_real_points	35
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Beta-arrestin-1
Molecular weight formula_weight	42177.2 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	12144

MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTAAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPSSVTLQPGPEDTGKAIGVDYEVKAFVAENLEEKIHKRNSVRLVIEKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADIVLFNTAQYKVPVAMEEADDTVAPSSTFSKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSSVAVELPFTLMHPKPKEEPPHREVPEHETPVDTNL

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Spodoptera frugiperda

Entity 2 Entity 2 polymer

Description description	scFv30
Molecular weight formula_weight	26986.7 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,F,D,E

SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKGTTAASGSSGGSSSGAEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGYTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVTVSSAHHHHHH

来源 Source

来源生物 organism	Bos taurus
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Spodoptera frugiperda

Entity 3 Entity 3 polymer

Description description	Adhesion G protein-coupled receptor E1
Molecular weight formula_weight	1563.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

ANLAIIMASGELTME

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Spodoptera frugiperda

Entity 4 Entity 4 polymer

Description description	Adhesion G protein-coupled receptor E1
Molecular weight formula_weight	32333.8 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	R,H

FSLYIISHVGTVISLVCLALAIATFLLCRAVQNHNTYMHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVLVVIISASVQPRGYGMHNRCWLNTETGFIWSFLGPVCMIITINSVLLAWTLWVLRQKLCSVSSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAWLFTIINSLQGAFIFLIHCLLNRQVRDEYKKLLTRKTDLSSHSQTSGILLSSMPSTSKMG

来源 Source

来源生物 organism	Mus musculus
通用名 common_name	house mouse
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Spodoptera frugiperda

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8. Citations (1)

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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	—

Resolution resolution	3.580 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.58 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	140558

fit	/app/data/saxs_computation/uc/9uco/9uco.fit
pddf	/app/data/pr_computation/uc/9uco/9uco.pr.out
profile	/app/data/saxs_computation/uc/9uco/9uco.dat

Cryo-EM structure of ADGRE1-beta arrestin1-scFv30 complex

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

Beta-arrestin-1

State in the Current Structure

Other States of the Same Protein in the Database

Adhesion G protein-coupled receptor E1

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

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

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)