› 3s37

X-ray diffraction
2.7Å resolution

Structural basis for the function of two anti-VEGF receptor antibodies

Released:
DOI: 10.2210/pdb3s37/pdb
PDB entry 3s37 coloured by chain, front view.
PDB entry 3s37 coloured by chain, side view.
PDB entry 3s37 coloured by chain, top view.
Source organisms:
Primary publication:
The structural basis for the function of two anti-VEGF receptor 2 antibodies.
Franklin MC, Navarro EC, Wang Y, Patel S, Singh P, Zhang Y, Persaud K, Bari A, Griffith H, Shen L, Balderes P, Kussie P
Structure 19 1097-107 (2011)
PMID: 21827946

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-543495 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
1121B Fab light chain Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.25 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
Structure domains: Immunoglobulins
1121B Fab heavy chain Chain: H
Molecule details ›
Chain: H
Length: 221 amino acids
Theoretical weight: 23.32 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Vascular endothelial growth factor receptor 2 Chain: X
Molecule details ›
Chain: X
Length: 122 amino acids
Theoretical weight: 13.5 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P35968 (Residues: 220-338; Coverage: 9%)
Gene names: FLK1, KDR, VEGFR2
Sequence domains: Immunoglobulin domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P43212
Unit cell:
a: 63.684Å b: 63.684Å c: 275.028Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.284 0.282 0.315
Expression systems:
  • Homo sapiens
  • Spodoptera frugiperda

Quick links

Citations

16 review citations

Advances in targeted therapy for esophageal cancer.
Yang et al. (2020)
15 more

3 mentions without citation

Biophysical Studies of the Induced Dimerization of Human VEGF Receptor 1 Binding Domain by Divalent Metals Competing with VEGF-A.
Gaucher et al. (2016)
2 more