6u1n

GPCR-Beta arrestin structure in lipid bilayer

Method: ELECTRON MICROSCOPY Dmax: 121.5 Å Quality: REASONABLE

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

Muscarinic acetylcholine receptor M2, Vasopressin V2 receptor chimera

Homo sapiens

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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 2–466 Fragment:M2 UNP residues 2-466 + V2 UNP residues 343-371 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P29066) Fab30 heavy chain × 1 (V9HW68) Fab30 light chain × 1 (Q7Z3Y4) 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

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.

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 1
Chains and sequence ranges Author chain R; PDBConstruct 9–473; UniProt 2–466

Muscarinic acetylcholine receptor M2, Vasopressin V2 receptor chimera

Homo sapiens

UniProt P30518

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 343–371 Fragment:M2 UNP residues 2-466 + V2 UNP residues 343-371 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P29066) Fab30 heavy chain × 1 (V9HW68) Fab30 light chain × 1 (Q7Z3Y4) 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

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.

36 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V2R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 481–509; UniProt 343–371

Beta-arrestin-1

Rattus norvegicus

UniProt P29066

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–393 Not recorded Muscarinic acetylcholine receptor M2, Vasopressin V2 receptor chimera × 1 (P08172,P30518) Fab30 heavy chain × 1 (V9HW68) Fab30 light chain × 1 (Q7Z3Y4) 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

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.

16 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 10–401; UniProt 2–393

Fab30 heavy chain

Homo sapiens

UniProt V9HW68

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 130–247 Not recorded Muscarinic acetylcholine receptor M2, Vasopressin V2 receptor chimera × 1 (P08172,P30518) Beta-arrestin-1 × 1 (P29066) Fab30 light chain × 1 (Q7Z3Y4) 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

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V9HW68_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 113–230; UniProt 130–247

Fab30 light chain

Homo sapiens

UniProt Q7Z3Y4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain L; UniProt 127–236 Not recorded Muscarinic acetylcholine receptor M2, Vasopressin V2 receptor chimera × 1 (P08172,P30518) Beta-arrestin-1 × 1 (P29066) Fab30 heavy chain × 1 (V9HW68) 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

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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7Z3Y4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain L; PDBConstruct 106–215; UniProt 127–236

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

SAXS profile for 6u1n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6u1n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6u1n
Deposition date deposition_date2019-08-16
Structure title titleGPCR-Beta arrestin structure in lipid bilayer
Keywords keywordsArrestin, GPCR, complex, signaling, SIGNALING PROTEIN-IMMUNE SYSTEM complex; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.26
Radius of gyration Rg (electron density) rg_electron35.73
Forward intensity I(0) i0111182000.00
Molecular weight molecular_weight82781.0 kDa
Excluded volume excluded_volume102790 ų
Envelope volume envelope_volume145150 ų
Hydration-shell volume shell_volume36504 ų
Envelope diameter envelope_diameter130.1
Shell Rg shell_rg38.94
Envelope Rg envelope_rg35.46
Shape Rg shape_rg35.76
Total Rg total_rg35.88
Total atoms total_atoms5863
Residues n_residues858
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax121.5
Rg (real space) rg_real36.43
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.1120e+08
I(0) uncertainty (real space) i0_real_error1.8340e+06
Rg (reciprocal space) rg_reciprocal36.33
I(0) (reciprocal space) i0_reciprocal111200000.0000
Solution quality estimate total_estimate0.6473
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13440000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 0.028; Positv: 1.000; Valcen: 0.876; Smooth: 0.776

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)