9lxr

A Cryo-EM structure of LA-PTH-PTH1R-Beta-arrestin1 complex (state 1 conformation)

Method: ELECTRON MICROSCOPY Dmax: 164.8 Å Quality: REASONABLE

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

Beta-arrestin-1

Homo sapiens

UniProt P49407

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 4–376 Not recorded Fab30H × 1 Fab30L × 1 LA-PTH × 1 Parathyroid hormone/parathyroid hormone-related peptide receptor × 1 (Q03431) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARRB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 2–374; UniProt 4–376

Parathyroid hormone/parathyroid hormone-related peptide 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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 27–507 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-arrestin-1 × 1 (P49407) Fab30H × 1 Fab30L × 1 LA-PTH × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.04 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.07 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 1–481; UniProt 27–507

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 9lxr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9lxr
Deposition date deposition_date2025-02-19
Structure title titleA Cryo-EM structure of LA-PTH-PTH1R-Beta-arrestin1 complex (state 1 conformation)
Keywords keywordsPTH1R, arrestin, GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.79
Radius of gyration Rg (electron density) rg_electron44.36
Forward intensity I(0) i0211160000.00
Molecular weight molecular_weight121650.0 kDa
Excluded volume excluded_volume153590 ų
Envelope volume envelope_volume211010 ų
Hydration-shell volume shell_volume43592 ų
Envelope diameter envelope_diameter172.0
Shell Rg shell_rg43.24
Envelope Rg envelope_rg44.96
Shape Rg shape_rg44.36
Total Rg total_rg44.27
Total atoms total_atoms8572
Residues n_residues1088
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 dmax164.8
Rg (real space) rg_real44.39
Rg uncertainty (real space) rg_real_error2.15
I(0) (real space) i0_real2.1120e+08
I(0) uncertainty (real space) i0_real_error4.4060e+06
Rg (reciprocal space) rg_reciprocal43.80
I(0) (reciprocal space) i0_reciprocal211000000.0000
Solution quality estimate total_estimate0.5463
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.6
Skewness Skewness skewness0.649
Kurtosis Kurtosis kurtosis0.029
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15660000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.593; Stabil: 1.000; Sysdev: 0.032; Positv: 1.000; Valcen: 0.503; Smooth: 0.718

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)