6z13

VEGF-A 13:107 crystallized with 3C bicyclic peptide

Method: X-RAY DIFFRACTION Dmax: 71.2 Å Quality: GOOD

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain V; UniProt 39–133 Chain W; UniProt 39–133 Not recorded bicyclic peptide 3C × 1 NH2 AMINO GROUP × 1 ACY ACETIC ACID × 5 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;(VEGF)2:2 peptide_3C complex purified on SEC and concentrated at 9.8mg/ml in Tris/HCl 10mM pH 8.5. Mix of 1ul of complex with 1 ul of reservoir : NaOAc/HCl 100mM pH 4.6 / MPD 36% (v/v) / CaCl2 20mM Resolution 1.80 Å R-free 0.247

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
PDB entities 2
Chains and sequence ranges Author chain V; PDBConstruct 1–95; UniProt 39–133 Author chain W; PDBConstruct 1–95; UniProt 39–133

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 6z13

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6z13
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6z13
Deposition date deposition_date2020-05-12
Structure title titleVEGF-A 13:107 crystallized with 3C bicyclic peptide
Keywords keywordsgrowth factor, peptide ligand, lactam bridge, alpha-helix stabilization, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.66
Radius of gyration Rg (electron density) rg_electron20.12
Forward intensity I(0) i011394100.00
Molecular weight molecular_weight24687.0 kDa
Excluded volume excluded_volume30548 ų
Envelope volume envelope_volume37294 ų
Hydration-shell volume shell_volume15976 ų
Envelope diameter envelope_diameter70.6
Shell Rg shell_rg25.89
Envelope Rg envelope_rg20.30
Shape Rg shape_rg20.17
Total Rg total_rg20.78
Total atoms total_atoms3344
Residues n_residues204
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 dmax71.2
Rg (real space) rg_real20.72
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.1390e+07
I(0) uncertainty (real space) i0_real_error1.3060e+05
Rg (reciprocal space) rg_reciprocal20.71
I(0) (reciprocal space) i0_reciprocal11390000.0000
Solution quality estimate total_estimate0.8757
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.221
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1320000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)