› 1kmx

Solution NMR

Heparin-binding Domain from Vascular Endothelial Growth Factor

Released:
DOI: 10.2210/pdb1kmx/pdb
PDB entry 1kmx coloured by chain, ensemble of 20 models, front view.
PDB entry 1kmx coloured by chain, ensemble of 20 models, side view.
PDB entry 1kmx coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Refinement of the solution structure of the heparin-binding domain of vascular endothelial growth factor using residual dipolar couplings.
Stauffer ME, Skelton NJ, Fairbrothe WJ
J Biomol NMR 23 57-61 (2002)
PMID: 12061718

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147426 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-VEGF Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P15692 (Residues: 346-395; Coverage: 13%)
Gene names: VEGF, VEGFA
Structure domains: Vascular endothelial growth factor, heparin-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Systems biology of vascular endothelial growth factors.
Mac Gabhann et al. (2008)
1 more

6 mentions without citation

Chemistry, structure and function of approved oligonucleotide therapeutics.
Egli et al. (2023)
5 more