7ll9

D-Protein RFX-V2 Bound to the VEGFR1 Domain 3 Site on VEGF-A

Method: X-RAY DIFFRACTION Dmax: 99.8 Å Quality: EXCELLENT

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

Isoform L-VEGF189 of Vascular endothelial growth factor A

Homo sapiens

UniProt P15692

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 214–315 Chain B; UniProt 214–315 Chain E; UniProt 214–315 Chain F; UniProt 214–315 Not recorded RFX-V2 × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291.2 K;magnesium chloride, Bis-Tris, PEG3350 Resolution 2.90 Å R-free 0.315

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.

50 other PDB entries and 72 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VEGFA_HUMAN
Isoform P15692-13
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–103; UniProt 214–315 Author chain B; PDBConstruct 2–103; UniProt 214–315 Author chain E; PDBConstruct 2–103; UniProt 214–315 Author chain F; PDBConstruct 2–103; UniProt 214–315

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 7ll9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ll9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ll9
Deposition date deposition_date2021-02-03
Structure title titleD-Protein RFX-V2 Bound to the VEGFR1 Domain 3 Site on VEGF-A
Keywords keywordsD-protein, Antagonist, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.95
Radius of gyration Rg (electron density) rg_electron31.31
Forward intensity I(0) i083356200.00
Molecular weight molecular_weight70397.0 kDa
Excluded volume excluded_volume87824 ų
Envelope volume envelope_volume129440 ų
Hydration-shell volume shell_volume35951 ų
Envelope diameter envelope_diameter105.5
Shell Rg shell_rg37.10
Envelope Rg envelope_rg29.86
Shape Rg shape_rg31.31
Total Rg total_rg31.89
Total atoms total_atoms4909
Residues n_residues389
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 dmax99.8
Rg (real space) rg_real31.87
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real8.3360e+07
I(0) uncertainty (real space) i0_real_error1.3320e+06
Rg (reciprocal space) rg_reciprocal31.91
I(0) (reciprocal space) i0_reciprocal83360000.0000
Solution quality estimate total_estimate0.9077
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.9
Skewness Skewness skewness0.201
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4991000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)