3v6b

VEGFR-2/VEGF-E complex structure

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: REASONABLE

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

VEGF-E

Orf virus

UniProt Q2F842

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 21–133 Fragment:VEGF-E, UNP residues 21-133 Vascular endothelial growth factor receptor 2 × 2 (P35968) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1 M HEPES (pH 6.5), 0.8 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.21 Å R-free 0.276

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q2F842_ORFV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–137; UniProt 21–133

Vascular endothelial growth factor receptor 2

Homo sapiens

UniProt P35968

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 132–548 Fragment:VEGFR-2, UNP residues 132-548 Mutation:Ig-domains 2-3 VEGF-E × 2 (Q2F842) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1 M HEPES (pH 6.5), 0.8 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 3.21 Å R-free 0.276

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.

53 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VGFR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 2–418; UniProt 132–548

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 3v6b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3v6b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3v6b
Deposition date deposition_date2011-12-19
Structure title titleVEGFR-2/VEGF-E complex structure
Keywords keywords;Ig-homology domain, VEGFR-2, growth factor receptor, VEGF ligand, ANGIOGENESIS, MEMBRANE, VEGF-E, Orf virus, HORMONE-SIGNALING PROTEIN complex ;; HORMONE/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.65
Radius of gyration Rg (electron density) rg_electron26.11
Forward intensity I(0) i016404800.00
Molecular weight molecular_weight29913.0 kDa
Excluded volume excluded_volume37087 ų
Envelope volume envelope_volume50358 ų
Hydration-shell volume shell_volume17962 ų
Envelope diameter envelope_diameter99.3
Shell Rg shell_rg30.20
Envelope Rg envelope_rg26.55
Shape Rg shape_rg26.14
Total Rg total_rg26.53
Total atoms total_atoms2093
Residues n_residues281
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 dmax94.2
Rg (real space) rg_real28.09
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.6510e+07
I(0) uncertainty (real space) i0_real_error2.3840e+05
Rg (reciprocal space) rg_reciprocal26.72
I(0) (reciprocal space) i0_reciprocal16400000.0000
Solution quality estimate total_estimate0.6142
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.424
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha4.0730
Highest regularization parameter α highest_alpha1615000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 0.848; Sysdev: 0.000; Positv: 1.000; Valcen: 0.608; Smooth: 0.493

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3v6bA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3v6bR01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3v6bR02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)