4qxf

crystal structure of human LGR4 and Rspo1

Method: X-RAY DIFFRACTION Dmax: 117.0 Å Quality: GOOD

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

Leucine-rich repeat-containing G-protein coupled receptor 4, Variable lymphocyte receptor B

Eptatretus burgeri

UniProt Q4G1L2

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 128–200 Fragment:UNP residues 27-252, UNP residues 128-200 Mutation:D75G R-spondin-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 128–200 Fragment:UNP residues 27-252, UNP residues 128-200 Mutation:D75G R-spondin-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243

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 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q4G1L2_EPTBU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 229–301; UniProt 128–200 Author chain B; PDBConstruct 229–301; UniProt 128–200

Leucine-rich repeat-containing G-protein coupled receptor 4, Variable lymphocyte receptor B

Eptatretus burgeri

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–252 Fragment:UNP residues 27-252, UNP residues 128-200 Mutation:D75G R-spondin-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 27–252 Fragment:UNP residues 27-252, UNP residues 128-200 Mutation:D75G R-spondin-1 × 1 (Q2MKA7) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LGR4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–228; UniProt 27–252 Author chain B; PDBConstruct 3–228; UniProt 27–252

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 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 34–135 Fragment:UNP residues 34-135 Leucine-rich repeat-containing G-protein coupled receptor 4, Variable lymphocyte receptor B × 1 (Q9BXB1,Q4G1L2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243
2 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 34–135 Fragment:UNP residues 34-135 Leucine-rich repeat-containing G-protein coupled receptor 4, Variable lymphocyte receptor B × 1 (Q9BXB1,Q4G1L2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.1M MES pH 6.5, 0.2M sodium thiocyanate, 22% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.25 Å R-free 0.243

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 16 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 1–102; UniProt 34–135 Author chain E; PDBConstruct 1–102; UniProt 34–135

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 4qxf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4qxf
Deposition date deposition_date2014-07-20
Structure title titlecrystal structure of human LGR4 and Rspo1
Keywords keywordsligand-receptor complex, LRR repeats, Beta-Hairpins, Glucosylation, Cell Membrane, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.91
Radius of gyration Rg (electron density) rg_electron34.42
Forward intensity I(0) i0111504000.00
Molecular weight molecular_weight83658.0 kDa
Excluded volume excluded_volume104630 ų
Envelope volume envelope_volume141660 ų
Hydration-shell volume shell_volume36117 ų
Envelope diameter envelope_diameter125.6
Shell Rg shell_rg38.66
Envelope Rg envelope_rg34.55
Shape Rg shape_rg34.34
Total Rg total_rg35.02
Total atoms total_atoms5859
Residues n_residues758
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 dmax117.0
Rg (real space) rg_real35.00
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real1.1150e+08
I(0) uncertainty (real space) i0_real_error1.8420e+06
Rg (reciprocal space) rg_reciprocal34.95
I(0) (reciprocal space) i0_reciprocal111500000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary114.4
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13710000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4qxfc_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.9 — Growth factor receptor domain
Family Family familyg.3.9.1 — Growth factor receptor domain
Domain ID domain_idd4qxfe_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.9 — Growth factor receptor domain
Family Family familyg.3.9.1 — Growth factor receptor domain

CATH v4.4 (2 domains)

Domain ID domain_id4qxfC00
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_id4qxfE00
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)