› 4lbb

X-ray diffraction
1.72Å resolution

Crystal structure of human alpha-defensin 1 (HNP1) I20A mutant

Released:
DOI: 10.2210/pdb4lbb/pdb
PDB entry 4lbb coloured by chain, front view.
PDB entry 4lbb coloured by chain, side view.
PDB entry 4lbb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function.
Zhao L, Tolbert WD, Ericksen B, Zhan C, Wu X, Yuan W, Li X, Pazgier M, Lu W
PLoS One 8 e78937 (2013)
PMID: 24236072

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil defensin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 30 amino acids
Theoretical weight: 3.41 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

1 bound ligand:
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P41
Unit cell:
a: 37.745Å b: 37.745Å c: 40.507Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.201 0.229
Expression system: Not provided

Quick links

Citations

5 review citations

Antiviral Activities of Human Host Defense Peptides.
Brice et al. (2020)
4 more

1 mention without citation

Single, double and quadruple alanine substitutions at oligomeric interfaces identify hydrophobicity as the key determinant of human neutrophil alpha defensin HNP1 function.
Zhao et al. (2013)