› 6s6m

X-ray diffraction
1.35Å resolution

Crystal structure of the human LL37(17-29) antimicrobial peptide

Released:
DOI: 10.2210/pdb6s6m/pdb
PDB entry 6s6m coloured by chain, front view.
PDB entry 6s6m coloured by chain, side view.
PDB entry 6s6m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure.
Engelberg Y, Landau M
OpenAccess logo Nat Commun 11 3894 (2020)
PMID: 32753597

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 340-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antibacterial peptide KR-20 Chains: A, B
Molecule details ›
Chains: A, B
Length: 13 amino acids
Theoretical weight: 1.72 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P49913 (Residues: 150-162; Coverage: 9%)
Gene names: CAMP, CAP18, FALL39, HSD26
Sequence domains: LPS binding domain of CAP18 (C terminal)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: P6122
Unit cell:
a: 41.45Å b: 41.45Å c: 57.47Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.232 0.268
Expression system: Not provided

Quick links

Citations

11 review citations

Pore formation in regulated cell death.
Flores-Romero et al. (2020)
10 more

3 mentions without citation

The role of bacterial transport systems in the removal of host antimicrobial peptides in Gram-negative bacteria.
Blair et al. (2022)
2 more