› 1lke

X-ray diffraction
1.9Å resolution

ENGINEERED LIPOCALIN DIGA16 IN COMPLEX WITH DIGOXIGENIN

Released:
DOI: 10.2210/pdb1lke/pdb
PDB entry 1lke coloured by chain, front view.
PDB entry 1lke coloured by chain, side view.
PDB entry 1lke coloured by chain, top view.
Source organism: Pieris brassicae
Primary publication:
Structural mechanism of specific ligand recognition by a lipocalin tailored for the complexation of digoxigenin.
Korndörfer IP, Schlehuber S, Skerra A
J Mol Biol 330 385-96 (2003)
PMID: 12823976

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bilin-binding protein Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.83 KDa
Source organism: Pieris brassicae
Expression system: Escherichia coli
UniProt:
  • Canonical: P09464 (Residues: 16-189; Coverage: 100%)
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand DOG 1 x DOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 75.052Å b: 63.988Å c: 39.452Å
α: 90° β: 91.53° γ: 90°
R-values:
R R work R free
0.188 0.185 0.248
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Engineering novel binding proteins from nonimmunoglobulin domains.
Binz et al. (2005)
9 more

4 mentions without citation

Structural insights for engineering binding proteins based on non-antibody scaffolds.
Gilbreth et al. (2012)
3 more