› 1kxo

X-ray diffraction
1.8Å resolution

ENGINEERED LIPOCALIN DIGA16 : APO-FORM

Released:
DOI: 10.2210/pdb1kxo/pdb
PDB entry 1kxo coloured by chain, front view.
PDB entry 1kxo coloured by chain, side view.
PDB entry 1kxo 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 73.873Å b: 63.476Å c: 38.191Å
α: 90° β: 92.02° γ: 90°
R-values:
R R work R free
0.212 0.209 0.289
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

4 mentions without citation

Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure-function insights.
Reis et al. (2006)
3 more