4bsk

Crystal structure of VEGF-C in complex with VEGFR-3 domains D1-2

Method: X-RAY DIFFRACTION Dmax: 114.1 Å Quality: REASONABLE

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

VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 3

HOMO SAPIENS

UniProt P35916

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 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 23–229 Fragment:LIGAND-BINDING DOMAINS D1-2, RESIDUES 23-229 VASCULAR ENDOTHELIAL GROWTH FACTOR C × 2 (P49767) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;SITTING DROPS AT ROOM TEMPERATURE OVER A RESERVOIR SOLUTION OF 0.1 M BIS-TRIS BUFFER AT PH 8.5-9.5 AND 1.0-1.5 M AMMONIUM SULPHATE. Resolution 4.20 Å R-free 0.372

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGFR3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–207; UniProt 23–229

VASCULAR ENDOTHELIAL GROWTH FACTOR C

HOMO SAPIENS

UniProt P49767

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 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 103–215 Fragment:VEGF HOMOLOGY DOMAIN, RESIDUES 103-215 Mutation:YES VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 3 × 2 (P35916) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;SITTING DROPS AT ROOM TEMPERATURE OVER A RESERVOIR SOLUTION OF 0.1 M BIS-TRIS BUFFER AT PH 8.5-9.5 AND 1.0-1.5 M AMMONIUM SULPHATE. Resolution 4.20 Å R-free 0.372

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–115; UniProt 103–215

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 4bsk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4bsk
Deposition date deposition_date2013-06-10
Structure title titleCrystal structure of VEGF-C in complex with VEGFR-3 domains D1-2
Keywords keywords;TRANSFERASE-HORMONE COMPLEX, TRANSFERASE, LYMPHANGIOGENESIS, ANGIOGENESIS, IG DOMAIN, GLYCOPROTEIN, RECEPTOR TYROSINE KINASE, DIMERIZATION ;; TRANSFERASE/HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.98
Radius of gyration Rg (electron density) rg_electron31.15
Forward intensity I(0) i013901300.00
Molecular weight molecular_weight26685.0 kDa
Excluded volume excluded_volume32622 ų
Envelope volume envelope_volume49601 ų
Hydration-shell volume shell_volume17076 ų
Envelope diameter envelope_diameter119.4
Shell Rg shell_rg30.05
Envelope Rg envelope_rg31.15
Shape Rg shape_rg31.20
Total Rg total_rg30.88
Total atoms total_atoms1876
Residues n_residues270
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 dmax114.1
Rg (real space) rg_real30.74
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.3900e+07
I(0) uncertainty (real space) i0_real_error2.4960e+05
Rg (reciprocal space) rg_reciprocal30.41
I(0) (reciprocal space) i0_reciprocal13900000.0000
Solution quality estimate total_estimate0.6950
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.770
Kurtosis Kurtosis kurtosis-0.004
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1095000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.345; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.092; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)