6t9d

Crystal structure of a bispecific DutaFab in complex with human VEGF121

Method: X-RAY DIFFRACTION Dmax: 103.5 Å Quality: EXCELLENT

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain CCC; UniProt 27–147 Chain DDD; UniProt 27–147 Not recorded VP mat DutaFab VH chain × 2 VP mat DutaFab VL chain × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;VEGFA-121 from Peprotech, catalogue number 100-20A, was mixed at a 1:1 molar ratio to VEGF monomer. The complex was concentrated to 11 mg/ml. Crystallization involved hanging drop vapour diffusion against 0.1 M MES pH 6.5 and 1.6 M magnesium sulphate. Crystals grew in about 120 days and were frozen in liquid nitrogen with 20 % glycerol as cryoprotectant. Resolution 2.90 Å R-free 0.280

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 P15692-9
PDB entities 3
Chains and sequence ranges Author chain CCC; PDBConstruct 1–121; UniProt 27–147 Author chain DDD; PDBConstruct 1–121; UniProt 27–147

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 6t9d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6t9d
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6t9d
Deposition date deposition_date2019-10-28
Structure title titleCrystal structure of a bispecific DutaFab in complex with human VEGF121
Keywords keywordsmonoclonal antibody, bispecific antibody, Fab fragment, VEGF, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.36
Radius of gyration Rg (electron density) rg_electron32.73
Forward intensity I(0) i0210859000.00
Molecular weight molecular_weight114410.0 kDa
Excluded volume excluded_volume142260 ų
Envelope volume envelope_volume187990 ų
Hydration-shell volume shell_volume47473 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg40.07
Envelope Rg envelope_rg32.35
Shape Rg shape_rg32.71
Total Rg total_rg33.36
Total atoms total_atoms8047
Residues n_residues1033
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 dmax103.5
Rg (real space) rg_real33.24
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.1090e+08
I(0) uncertainty (real space) i0_real_error3.0800e+06
Rg (reciprocal space) rg_reciprocal33.31
I(0) (reciprocal space) i0_reciprocal210900000.0000
Solution quality estimate total_estimate0.9061
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.6
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.554
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22320000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)