› 1t0v

Solution NMR

NMR Solution Structure of the Engineered Lipocalin FluA(R95K) Northeast Structural Genomics Target OR17

Released:
DOI: 10.2210/pdb1t0v/pdb
PDB entry 1t0v coloured by chain, ensemble of 20 models, front view.
PDB entry 1t0v coloured by chain, ensemble of 20 models, side view.
PDB entry 1t0v coloured by chain, ensemble of 20 models, top view.
Source organism: Pieris brassicae
Primary publication:
NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding.
Mills JL, Liu G, Skerra A, Szyperski T
Biochemistry 48 7411-9 (2009)
PMID: 19603796

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: 21.03 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
Refinement method: torsion angle dynamics and simulated annealing (DYANA)
Expression system: Escherichia coli

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Citations

1 review citation

Survey of the year 2009: applications of isothermal titration calorimetry.
Falconer et al. (2011)
8 other articles

4 mentions without citation

Protein scaffold-based molecular probes for cancer molecular imaging.
Miao et al. (2011)
3 more