9khh

Structure of the complex of LGR4 with Norrin (2:2)

Method: ELECTRON MICROSCOPY Dmax: 179.8 Å Quality: GOOD

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

Norrin,Immunoglobulin gamma-1 heavy chain

Homo sapiens

UniProt P0DOX5

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 220–449 Chain F; UniProt 220–449 Not recorded MB52 × 2 Leucine-rich repeat-containing G-protein coupled receptor 4 × 2 (Q9BXB1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 172–401; UniProt 220–449 Author chain F; PDBConstruct 172–401; UniProt 220–449

Norrin,Immunoglobulin gamma-1 heavy chain

Homo sapiens

UniProt Q00604

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 25–133 Chain F; UniProt 25–133 Not recorded MB52 × 2 Leucine-rich repeat-containing G-protein coupled receptor 4 × 2 (Q9BXB1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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.

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

View Construct and Data Evidence
UniProt name NDP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 39–147; UniProt 25–133 Author chain F; PDBConstruct 39–147; UniProt 25–133

Leucine-rich repeat-containing G-protein coupled receptor 4

Homo sapiens

UniProt Q9BXB1

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 24–951 Chain D; UniProt 24–951 Not recorded MB52 × 2 Norrin,Immunoglobulin gamma-1 heavy chain × 2 (Q00604,P0DOX5) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.65 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.

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

View Construct and Data Evidence
UniProt name LGR4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 16–943; UniProt 24–951 Author chain D; PDBConstruct 16–943; UniProt 24–951

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 9khh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9khh
Deposition date deposition_date2024-11-10
Structure title titleStructure of the complex of LGR4 with Norrin (2:2)
Keywords keywordsLGR4 Norrin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.03
Radius of gyration Rg (electron density) rg_electron57.85
Forward intensity I(0) i0558234000.00
Molecular weight molecular_weight175480.0 kDa
Excluded volume excluded_volume210350 ų
Envelope volume envelope_volume383440 ų
Hydration-shell volume shell_volume56893 ų
Envelope diameter envelope_diameter189.5
Shell Rg shell_rg57.37
Envelope Rg envelope_rg58.36
Shape Rg shape_rg58.20
Total Rg total_rg56.81
Total atoms total_atoms12354
Residues n_residues1871
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 dmax179.8
Rg (real space) rg_real61.06
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real5.5820e+08
I(0) uncertainty (real space) i0_real_error1.1630e+07
Rg (reciprocal space) rg_reciprocal60.94
I(0) (reciprocal space) i0_reciprocal558100000.0000
Solution quality estimate total_estimate0.8336
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary89.9
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.759
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16240000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)