› 4du0

X-ray diffraction
1.9Å resolution

Crystal structure of human alpha-defensin 1, HNP1 (G17A mutant)

Released:
DOI: 10.2210/pdb4du0/pdb
PDB entry 4du0 coloured by chain, front view.
PDB entry 4du0 coloured by chain, side view.
PDB entry 4du0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Invariant gly residue is important for α-defensin folding, dimerization, and function: a case study of the human neutrophil α-defensin HNP1.
Zhao L, Ericksen B, Wu X, Zhan C, Yuan W, Li X, Pazgier M, Lu W
J Biol Chem 287 18900-12 (2012)
PMID: 22496447

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-157836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil defensin 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 30 amino acids
Theoretical weight: 3.47 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P59665 (Residues: 65-94; Coverage: 40%)
Gene names: DEF1, DEFA1, DEFA1B, DEFA2, MRS
Sequence domains: Mammalian defensin

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 38.453Å b: 50.083Å c: 78.883Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.175 0.212
Expression system: Not provided

Quick links

Citations

5 review citations

Defensins in innate immunity.
Zhao et al. (2014)
4 more

1 mention without citation

Invariant gly residue is important for α-defensin folding, dimerization, and function: a case study of the human neutrophil α-defensin HNP1.
Zhao et al. (2012)