9e51

Cryo-EM structure of human LPHN2 (ADGRL2)/G13 complex in lipid nanodiscs

Method: ELECTRON MICROSCOPY Dmax: 113.3 Å Quality: GOOD

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

Isoform 2 of Guanine nucleotide-binding protein subunit alpha-13

Homo sapiens

UniProt Q14344

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 108–282 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Adhesion G protein-coupled receptor L2 × 1 (O95490) CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNA13_HUMAN
Isoform Q14344-2
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 66–230; UniProt 108–282

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–340 Not recorded Isoform 2 of Guanine nucleotide-binding protein subunit alpha-13 × 1 (Q14344) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) Adhesion G protein-coupled receptor L2 × 1 (O95490) CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–340; UniProt 1–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Homo sapiens

UniProt P59768

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–71 Not recorded Isoform 2 of Guanine nucleotide-binding protein subunit alpha-13 × 1 (Q14344) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Adhesion G protein-coupled receptor L2 × 1 (O95490) CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

1233 other PDB entries and 1236 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–71; UniProt 1–71

Adhesion G protein-coupled receptor L2

Homo sapiens

UniProt O95490

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 825–1125 Not recorded Isoform 2 of Guanine nucleotide-binding protein subunit alpha-13 × 1 (Q14344) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P59768) CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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

View Construct and Data Evidence
UniProt name AGRL2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 2–302; UniProt 825–1125

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 9e51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e51
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e51
Deposition date deposition_date2024-10-26
Structure title titleCryo-EM structure of human LPHN2 (ADGRL2)/G13 complex in lipid nanodiscs
Keywords keywords;adhesion GPCR, Tethered agonist, Latrophilin-2, LPHN2 (ADGRL2), Heterotrimeric G protein, Cryo-EM, Lipid Nanodiscs, Membrane Protein, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.62
Radius of gyration Rg (electron density) rg_electron34.84
Forward intensity I(0) i0143636000.00
Molecular weight molecular_weight99163.0 kDa
Excluded volume excluded_volume125440 ų
Envelope volume envelope_volume166540 ų
Hydration-shell volume shell_volume41150 ų
Envelope diameter envelope_diameter120.9
Shell Rg shell_rg39.69
Envelope Rg envelope_rg34.64
Shape Rg shape_rg34.85
Total Rg total_rg35.21
Total atoms total_atoms6976
Residues n_residues882
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 dmax113.3
Rg (real space) rg_real34.70
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.4360e+08
I(0) uncertainty (real space) i0_real_error2.5500e+06
Rg (reciprocal space) rg_reciprocal34.65
I(0) (reciprocal space) i0_reciprocal143600000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25170000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.673

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)