1vpp

COMPLEX BETWEEN VEGF AND A RECEPTOR BLOCKING PEPTIDE

Method: X-RAY DIFFRACTION Dmax: 88.7 Å Quality: GOOD

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

PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR)

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 Fragment:RECEPTOR BINDING DOMAIN PROTEIN (PEPTIDE V108) × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;pH 7.5 Resolution 1.90 Å R-free 0.270

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 1–102; 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 1vpp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1vpp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1vpp
Deposition date deposition_date1998-10-09
Structure title titleCOMPLEX BETWEEN VEGF AND A RECEPTOR BLOCKING PEPTIDE
Keywords keywordsCYSTINE KNOT, ANGIOGENESIS, VASCULOGENESIS, RECEPTOR BLOCKING PEPTIDE, GROWTH FACTOR-GROWTH FACTOR INHIBITOR COMPLEX; GROWTH FACTOR/GROWTH FACTOR INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.54
Radius of gyration Rg (electron density) rg_electron22.11
Forward intensity I(0) i013039100.00
Molecular weight molecular_weight25978.0 kDa
Excluded volume excluded_volume31969 ų
Envelope volume envelope_volume41737 ų
Hydration-shell volume shell_volume16658 ų
Envelope diameter envelope_diameter89.1
Shell Rg shell_rg27.46
Envelope Rg envelope_rg22.58
Shape Rg shape_rg22.17
Total Rg total_rg22.69
Total atoms total_atoms1803
Residues n_residues224
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 dmax88.7
Rg (real space) rg_real22.74
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real1.3040e+07
I(0) uncertainty (real space) i0_real_error2.2130e+05
Rg (reciprocal space) rg_reciprocal22.70
I(0) (reciprocal space) i0_reciprocal13040000.0000
Solution quality estimate total_estimate0.7809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis0.014
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1456000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.548; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.511; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1vppv_
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
Domain ID domain_idd1vppw_
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 (2 domains)

Domain ID domain_id1vppV00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id1vppW00
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)