4bsr

Structure of the ectodomain of LGR5 in complex with R-spondin-1 (Fu1Fu2) in P22121 crystal form

Method: X-RAY DIFFRACTION Dmax: 142.2 Å Quality: REASONABLE

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 4 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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.20 Å R-free 0.258

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 4 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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.20 Å R-free 0.258

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 4bsr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4bsr
Deposition date deposition_date2013-06-11
Structure title titleStructure of the ectodomain of LGR5 in complex with R-spondin-1 (Fu1Fu2) in P22121 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_guinier40.78
Radius of gyration Rg (electron density) rg_electron40.85
Forward intensity I(0) i0264431000.00
Molecular weight molecular_weight132280.0 kDa
Excluded volume excluded_volume165690 ų
Envelope volume envelope_volume231690 ų
Hydration-shell volume shell_volume50411 ų
Envelope diameter envelope_diameter146.8
Shell Rg shell_rg43.06
Envelope Rg envelope_rg40.58
Shape Rg shape_rg40.80
Total Rg total_rg41.16
Total atoms total_atoms9274
Residues n_residues1170
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 dmax142.2
Rg (real space) rg_real41.11
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real2.6440e+08
I(0) uncertainty (real space) i0_real_error4.9810e+06
Rg (reciprocal space) rg_reciprocal40.78
I(0) (reciprocal space) i0_reciprocal264300000.0000
Solution quality estimate total_estimate0.6011
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.592
Kurtosis Kurtosis kurtosis-0.205
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38070000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.710; Stabil: 1.000; Sysdev: 0.107; Positv: 1.000; Valcen: 0.755; Smooth: 0.605

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4bsrA01
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id4bsrB01
Class class3 — Alpha Beta
Architecture architecture80 — Alpha-Beta Horseshoe
Topology topology10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Homologous superfamily homologous superfamily10 — Ribonuclease Inhibitor
Domain ID domain_id4bsrC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology220 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Homologous superfamily homologous superfamily10 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2
Domain ID domain_id4bsrD00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology220 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
Homologous superfamily homologous superfamily10 — Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2

8. Citations (1)

9. Files and Curves (10)