4bst

Structure of the ectodomain of LGR5 in complex with R-spondin-1 (Fu1Fu2) in P6122 crystal form

Method: X-RAY DIFFRACTION Dmax: 142.9 Å Quality: GOOD

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

LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN COUPLED RECEPTOR 5

HOMO SAPIENS

UniProt O75473

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 22–543 Chain B; UniProt 22–543 Fragment:EXTRACELLULAR LRR DOMAIN, RESIDUES 22-543 R-SPONDIN-1 × 2 (Q2MKA7) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.30 Å R-free 0.268

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.

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

View Construct and Data Evidence
UniProt name LGR5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–536; UniProt 22–543 Author chain B; PDBConstruct 15–536; UniProt 22–543

R-SPONDIN-1

HOMO SAPIENS

UniProt Q2MKA7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 31–146 Chain D; UniProt 31–146 Fragment:FU1FU2, RESIDUES 31-146 LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN COUPLED RECEPTOR 5 × 2 (O75473) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 4.30 Å R-free 0.268

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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RSPO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–118; UniProt 31–146 Author chain D; PDBConstruct 3–118; UniProt 31–146

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 4bst

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4bst
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4bst
Deposition date deposition_date2013-06-11
Structure title titleStructure of the ectodomain of LGR5 in complex with R-spondin-1 (Fu1Fu2) in P6122 crystal form
Keywords keywords;SIGNALING PROTEIN, ADULT STEM CELL, LEUCINE-RICH REPEAT G-PROTEIN COUPLED RECEPTOR, LEUCINE-RICH REPEAT, FURIN DOMAIN, WNT SIGNALING, CONGENITAL ANONYCHIA ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.66
Radius of gyration Rg (electron density) rg_electron40.77
Forward intensity I(0) i0239248000.00
Molecular weight molecular_weight126020.0 kDa
Excluded volume excluded_volume157890 ų
Envelope volume envelope_volume214700 ų
Hydration-shell volume shell_volume47087 ų
Envelope diameter envelope_diameter147.5
Shell Rg shell_rg42.59
Envelope Rg envelope_rg40.70
Shape Rg shape_rg40.72
Total Rg total_rg41.04
Total atoms total_atoms8833
Residues n_residues1122
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 dmax142.9
Rg (real space) rg_real41.04
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real2.3920e+08
I(0) uncertainty (real space) i0_real_error4.3420e+06
Rg (reciprocal space) rg_reciprocal40.67
I(0) (reciprocal space) i0_reciprocal239200000.0000
Solution quality estimate total_estimate0.7870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.6
Skewness Skewness skewness0.600
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40990000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.641; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.626; Smooth: 0.677

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)