1kmx

Heparin-binding Domain from Vascular Endothelial Growth Factor

Method: SOLUTION NMR Dmax: 39.7 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 137–191 Fragment:heparin-binding domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;300 K;Ionic strength (raw mmCIF value) 25 mM sodium acetate; 50 mM sodium chloride;Pressure ambient NMR measurement conditions:pH 5.5;300 K;Ionic strength (raw mmCIF value) 25 mM sodium acetate; 50 mM sodium chloride;Pressure ambient NMR measurement conditions:pH 5.5;300 K;Ionic strength (raw mmCIF value) 25 mM sodium acetate; 50 mM sodium chloride;Pressure ambient NMR measurement conditions:pH 5.5;300 K;Ionic strength (raw mmCIF value) 25 mM sodium acetate; 50 mM sodium chloride;Pressure ambient NMR sample composition:2.0 mM VEGF heparin-binding domain; 25 mM sodium acetate; 50 mM sodium chloride, 0.02% sodium azide | 90% H2O/10% D2O NMR sample composition:2.0 mM VEGF heparin-binding domain U-15N; 25 mM sodium acetate; 50 mM sodium chloride, 0.02% sodium azide | 90% H2O/10% D2O NMR sample composition:2.0 mM VEGF heparin-binding domain U-15N; 25 mM sodium acetate; 50 mM sodium chloride, 0.02% sodium azide | 99.9% D2O NMR sample composition:0.6 mM VEGF heparin-binding domain U-15N; 25 mM sodium acetate; 50 mM sodium chloride; 0.02% sodium azide | 4:1:0.2 ditridecanoyl-phosphatidylcholine/dihexanoyl-phosphatidylcholine/cetyltrimethylammonium bromide, 5% w/v total lipid in 90% H2O, 10% D2O Resolution not provided

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 A; PDBConstruct 1–55; UniProt 137–191

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 1kmx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kmx
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1kmx
Deposition date deposition_date2001-12-17
Structure title titleHeparin-binding Domain from Vascular Endothelial Growth Factor
Keywords keywordsheparin-binding, angiogenesis, growth factor, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.98
Radius of gyration Rg (electron density) rg_electron15.21
Forward intensity I(0) i0324415000.00
Molecular weight molecular_weight129110.0 kDa
Excluded volume excluded_volume153510 ų
Envelope volume envelope_volume28335 ų
Hydration-shell volume shell_volume13266 ų
Envelope diameter envelope_diameter70.9
Shell Rg shell_rg24.53
Envelope Rg envelope_rg20.76
Shape Rg shape_rg15.25
Total Rg total_rg15.37
Total atoms total_atoms17620
Residues n_residues1100
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 dmax39.7
Rg (real space) rg_real13.77
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real3.0840e+08
I(0) uncertainty (real space) i0_real_error2.5570e+06
Rg (reciprocal space) rg_reciprocal15.32
I(0) (reciprocal space) i0_reciprocal324400000.0000
Solution quality estimate total_estimate0.6754
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary12.6
Skewness Skewness skewness0.357
Kurtosis Kurtosis kurtosis-0.616
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha2.9260
Highest regularization parameter α highest_alpha91750.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.011; Oscil: 0.990; Stabil: 0.990; Sysdev: 0.000; Positv: 1.000; Valcen: 0.841; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1kmxa_
Class classg — Small proteins
Fold Fold foldg.25 — Heparin-binding domain from vascular endothelial growth factor
Superfamily Superfamily superfamilyg.25.1 — Heparin-binding domain from vascular endothelial growth factor
Family Family familyg.25.1.1 — Heparin-binding domain from vascular endothelial growth factor

CATH v4.4 (1 domains)

Domain ID domain_id1kmxA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology160 — Vascular Endothelial Growth Factor-165, Heparin-binding Domain
Homologous superfamily homologous superfamily10 — Vascular endothelial growth factor, heparin-binding domain

8. Citations (2)

9. Files and Curves (10)