3s1b

The Development of Peptide-based Tools for the Analysis of Angiogenesis

Method: X-RAY DIFFRACTION Dmax: 70.4 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain V; UniProt 38–133 Not recorded mini-Z × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;289 K;0.1 M NaOAc, 0.02 M CaCl2, MPD 30.0% v/v, pH 6.0, vapor diffusion, hanging drop, temperature 289K Resolution 2.90 Å R-free 0.251

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 1
Chains and sequence ranges Author chain V; PDBConstruct 1–96; UniProt 38–133

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 3s1b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3s1b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3s1b
Deposition date deposition_date2011-05-14
Structure title titleThe Development of Peptide-based Tools for the Analysis of Angiogenesis
Keywords keywordsVEGF, cystine knot, mini-Z, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.67
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i04659120.00
Molecular weight molecular_weight15198.0 kDa
Excluded volume excluded_volume18804 ų
Envelope volume envelope_volume26382 ų
Hydration-shell volume shell_volume11649 ų
Envelope diameter envelope_diameter69.4
Shell Rg shell_rg25.37
Envelope Rg envelope_rg21.38
Shape Rg shape_rg21.30
Total Rg total_rg22.00
Total atoms total_atoms1058
Residues n_residues130
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 dmax70.4
Rg (real space) rg_real21.86
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real4.6590e+06
I(0) uncertainty (real space) i0_real_error6.7660e+04
Rg (reciprocal space) rg_reciprocal21.83
I(0) (reciprocal space) i0_reciprocal4659000.0000
Solution quality estimate total_estimate0.8594
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.794
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha255700.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.586; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3s1bv_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.1 — Platelet-derived growth factor-like

CATH v4.4 (1 domains)

Domain ID domain_id3s1bV00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)