› 1ewf

X-ray diffraction
1.7Å resolution

THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI

Released:
DOI: 10.2210/pdb1ewf/pdb
PDB entry 1ewf coloured by chain, front view.
PDB entry 1ewf coloured by chain, side view.
PDB entry 1ewf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 1.7 A crystal structure of BPI: a study of how two dissimilar amino acid sequences can adopt the same fold.
Kleiger G, Beamer LJ, Grothe R, Mallick P, Eisenberg D
J Mol Biol 299 1019-34 (2000)
PMID: 10843855

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-147900 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bactericidal permeability-increasing protein Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 50.7 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P17213 (Residues: 32-487; Coverage: 100%)
Gene name: BPI
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PC1 2 x PC1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: C2
Unit cell:
a: 184.32Å b: 31.23Å c: 80.66Å
α: 90° β: 103.2° γ: 90°
R-values:
R R work R free
0.198 0.198 0.25
Expression system: Cricetulus griseus

Quick links

Citations

6 review citations

Recognition of lipopolysaccharide pattern by TLR4 complexes.
Park et al. (2013)
5 more

16 mentions without citation

A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.
Moon et al. (2010)
15 more