9lz2

Cryo-EM structure of PTH1R(V2RC)-beta-arrestin1 complex

Method: ELECTRON MICROSCOPY Dmax: 142.1 Å Quality: GOOD

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

Beta-arrestin-1

Bos taurus

UniProt P17870

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–393 Not recorded Long-acting PTH × 1 Fab30 heavy chain × 1 Fab30 light chain × 1 Parathyroid hormone/parathyroid hormone-related peptide receptor,Vasopressin V2 receptor × 1 (Q03431,P30518) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–393; UniProt 1–393

Parathyroid hormone/parathyroid hormone-related peptide receptor,Vasopressin V2 receptor

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 343–368 Non-standard monomer:Yes (specific site not provided by mmCIF) Long-acting PTH × 1 Beta-arrestin-1 × 1 (P17870) Fab30 heavy chain × 1 Fab30 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 5
Chains and sequence ranges Author chain R; PDBConstruct 475–500; UniProt 343–368

Parathyroid hormone/parathyroid hormone-related peptide receptor,Vasopressin V2 receptor

Homo sapiens

UniProt Q03431

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 27–490 Non-standard monomer:Yes (specific site not provided by mmCIF) Long-acting PTH × 1 Beta-arrestin-1 × 1 (P17870) Fab30 heavy chain × 1 Fab30 light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

43 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTH1R_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 1–464; UniProt 27–490

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 9lz2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lz2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lz2
Deposition date deposition_date2025-02-21
Structure title titleCryo-EM structure of PTH1R(V2RC)-beta-arrestin1 complex
Keywords keywordsCryo-EM structure, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.90
Radius of gyration Rg (electron density) rg_electron36.90
Forward intensity I(0) i0148105000.00
Molecular weight molecular_weight101000.0 kDa
Excluded volume excluded_volume127760 ų
Envelope volume envelope_volume167190 ų
Hydration-shell volume shell_volume40092 ų
Envelope diameter envelope_diameter152.1
Shell Rg shell_rg40.18
Envelope Rg envelope_rg36.82
Shape Rg shape_rg36.90
Total Rg total_rg37.16
Total atoms total_atoms7117
Residues n_residues884
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 dmax142.1
Rg (real space) rg_real37.16
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.4810e+08
I(0) uncertainty (real space) i0_real_error2.5270e+06
Rg (reciprocal space) rg_reciprocal37.00
I(0) (reciprocal space) i0_reciprocal148100000.0000
Solution quality estimate total_estimate0.8053
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.7
Skewness Skewness skewness0.516
Kurtosis Kurtosis kurtosis-0.044
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17230000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.634; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)