4qxe

Crystal structure of LGR4 fused with hagfish VLR

Method: X-RAY DIFFRACTION Dmax: 100.5 Å Quality: REASONABLE

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

Leucine-rich repeat-containing G-protein coupled receptor 4, linker, 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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 133–200 Fragment:R-spondin Receptor, UNP residues 27-396, UNP residues 133-200 Mutation:D75G NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 CL CHLORIDE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M HEPES pH 7.5, 2.0M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.20 Å R-free 0.237

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 50 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 375–442; UniProt 133–200

Leucine-rich repeat-containing G-protein coupled receptor 4, linker, 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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–396 Fragment:R-spondin Receptor, UNP residues 27-396, UNP residues 133-200 Mutation:D75G NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 CL CHLORIDE ION × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;289 K;0.1M HEPES pH 7.5, 2.0M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.20 Å R-free 0.237

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 1
Chains and sequence ranges Author chain A; PDBConstruct 3–372; UniProt 27–396

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 4qxe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4qxe
Deposition date deposition_date2014-07-20
Structure title titleCrystal structure of LGR4 fused with hagfish VLR
Keywords keywordsLRR repeats, Receptor, R-spondins, Glycosylation, 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_guinier30.95
Radius of gyration Rg (electron density) rg_electron30.58
Forward intensity I(0) i040095800.00
Molecular weight molecular_weight49709.0 kDa
Excluded volume excluded_volume62155 ų
Envelope volume envelope_volume81794 ų
Hydration-shell volume shell_volume23603 ų
Envelope diameter envelope_diameter110.5
Shell Rg shell_rg35.87
Envelope Rg envelope_rg30.63
Shape Rg shape_rg30.52
Total Rg total_rg31.27
Total atoms total_atoms3490
Residues n_residues443
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 dmax100.5
Rg (real space) rg_real31.24
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real4.0100e+07
I(0) uncertainty (real space) i0_real_error6.2880e+05
Rg (reciprocal space) rg_reciprocal31.13
I(0) (reciprocal space) i0_reciprocal40090000.0000
Solution quality estimate total_estimate0.5086
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.676
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10930000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 0.994; Sysdev: 0.040; Positv: 1.000; Valcen: 0.545; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4qxeA01
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

8. Citations (1)

9. Files and Curves (10)