› 2nlq

X-ray diffraction
1.8Å resolution

Human beta-defensin-1 (Mutant Lys31Ala)

Released:
DOI: 10.2210/pdb2nlq/pdb
PDB entry 2nlq coloured by chain, front view.
PDB entry 2nlq coloured by chain, side view.
PDB entry 2nlq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Studies of the biological properties of human beta-defensin 1.
Pazgier M, Prahl A, Hoover DM, Lubkowski J
J Biol Chem 282 1819-29 (2007)
PMID: 17071614

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-157949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-defensin 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 36 amino acids
Theoretical weight: 3.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60022 (Residues: 33-68; Coverage: 77%)
Gene names: BD1, DEFB1, HBD1
Sequence domains: Beta defensin

Ligands and Environments

3 bound ligands:
Ligand SO4 5 x SO4
Ligand GLY 1 x GLY
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 97.89Å b: 27.68Å c: 58.26Å
α: 90° β: 113.5° γ: 90°
R-values:
R R work R free
0.183 0.179 0.257
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Topical antimicrobials for burn wound infections.
Dai et al. (2010)
4 more

1 mention without citation

Statistical analysis of interface similarity in crystals of homologous proteins.
Xu et al. (2008)