› 1dfn

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF DEFENSIN HNP-3, AN AMPHIPHILIC DIMER: MECHANISMS OF MEMBRANE PERMEABILIZATION

Released:
DOI: 10.2210/pdb1dfn/pdb
PDB entry 1dfn coloured by chain, front view.
PDB entry 1dfn coloured by chain, side view.
PDB entry 1dfn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization.
Hill CP, Yee J, Selsted ME, Eisenberg D
Science 251 1481-5 (1991)
PMID: 2006422

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-157841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil defensin 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 30 amino acids
Theoretical weight: 3.5 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P59666 (Residues: 65-94; Coverage: 40%)
Gene names: DEF3, DEFA3
Sequence domains: Mammalian defensin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 30.8Å b: 45Å c: 40.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

69 review citations

Defensins: antimicrobial peptides of innate immunity.
Ganz T. (2003)
68 more

21 mentions without citation

A functional-phylogenetic classification system for transmembrane solute transporters.
Saier MH. (2000)
20 more