› 1bp1

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN

Released:
DOI: 10.2210/pdb1bp1/pdb
PDB entry 1bp1 coloured by chain, front view.
PDB entry 1bp1 coloured by chain, side view.
PDB entry 1bp1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution.
Beamer LJ, Carroll SF, Eisenberg D
Science 276 1861-4 (1997)
PMID: 9188532

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: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 185.6Å b: 33Å c: 85.2Å
α: 90° β: 101.6° γ: 90°
R-values:
R R work R free
0.225 0.225 0.295
Expression system: Cricetulus griseus

Quick links

Citations

74 review citations

Diversity of antimicrobial peptides and their mechanisms of action.
Epand et al. (1999)
73 more

17 mentions without citation

Host Defense Proteins and Peptides with Lipopolysaccharide-Binding Activity from Marine Invertebrates and Their Therapeutic Potential in Gram-Negative Sepsis.
Solov'eva et al. (2023)
16 more