3s1k

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

Method: X-RAY DIFFRACTION Dmax: 87.8 Å Quality: REASONABLE

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 34–135 Chain W; UniProt 34–135 Not recorded Z-domain × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;289 K;0.2 M KI, 0.1 M MES, PEG 4000 25.0% v/v, pH 6.5, vapor diffusion, hanging drop, temperature 289K Resolution 2.55 Å R-free 0.271

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 1–102; UniProt 34–135 Author chain W; PDBConstruct 1–102; UniProt 34–135

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 3s1k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3s1k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3s1k
Deposition date deposition_date2011-05-15
Structure title titleThe Development of Peptide-based Tools for the Analysis of Angiogenesis
Keywords keywordsVEGF, cystine knot, Z-domain, phage-display, cystine-knot, 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_guinier24.38
Radius of gyration Rg (electron density) rg_electron24.11
Forward intensity I(0) i020201500.00
Molecular weight molecular_weight33525.0 kDa
Excluded volume excluded_volume41536 ų
Envelope volume envelope_volume51726 ų
Hydration-shell volume shell_volume18909 ų
Envelope diameter envelope_diameter88.0
Shell Rg shell_rg29.69
Envelope Rg envelope_rg24.10
Shape Rg shape_rg24.16
Total Rg total_rg24.62
Total atoms total_atoms2342
Residues n_residues292
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 dmax87.8
Rg (real space) rg_real24.59
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real2.0200e+07
I(0) uncertainty (real space) i0_real_error2.9870e+05
Rg (reciprocal space) rg_reciprocal24.54
I(0) (reciprocal space) i0_reciprocal20200000.0000
Solution quality estimate total_estimate0.7461
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.513
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2207000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.691; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.623; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3s1kw_
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 (4 domains)

Domain ID domain_id3s1kA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id3s1kB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id3s1kV00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3s1kW00
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)