› 4y5v

X-ray diffraction
2.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-210750 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
diabody 305 VH domain Chains: A, D, G
Molecule details ›
Chains: A, D, G
Length: 130 amino acids
Theoretical weight: 13.82 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
Structure domains: Immunoglobulins
Diabody 305 VL domain Chains: B, E, H
Molecule details ›
Chains: B, E, H
Length: 117 amino acids
Theoretical weight: 12.08 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
Structure domains: Immunoglobulins
Erythropoietin receptor Chains: C, F, I
Molecule details ›
Chains: C, F, I
Length: 229 amino acids
Theoretical weight: 25.13 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P19235 (Residues: 32-249; Coverage: 45%)
Gene name: EPOR
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

3 bound ligands:
Ligand GOL 15 x GOL
Ligand PGE 1 x PGE
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: C2221
Unit cell:
a: 125.73Å b: 215.021Å c: 171.905Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.229
Expression system: Trichoplusia ni

Quick links

Citations

26 review citations

Pathogenesis of myeloproliferative neoplasms.
Skoda et al. (2015)
25 more

1 mention without citation

Crystal structures of mono- and bi-specific diabodies and reduction of their structural flexibility by introduction of disulfide bridges at the Fv interface.
Kim et al. (2016)