› 5nnk

X-ray diffraction
1.8Å resolution

The structure of LL-37 crystallized in the presence LDAO

Released:
DOI: 10.2210/pdb5nnk/pdb
PDB entry 5nnk coloured by chain, front view.
PDB entry 5nnk coloured by chain, side view.
PDB entry 5nnk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural remodeling and oligomerization of human cathelicidin on membranes suggest fibril-like structures as active species.
Sancho-Vaello E, François P, Bonetti EJ, Lilie H, Finger S, Gil-Ortiz F, Gil-Carton D, Zeth K
Sci Rep 7 15371 (2017)
PMID: 29133814

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antibacterial peptide LL-37 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 4.5 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P49913 (Residues: 134-170; Coverage: 26%)
Gene names: CAMP, CAP18, FALL39, HSD26
Sequence domains: LPS binding domain of CAP18 (C terminal)

Ligands and Environments

1 bound ligand:
Ligand LDA 3 x LDA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: I4122
Unit cell:
a: 43.309Å b: 43.309Å c: 109.819Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.252 0.268
Expression system: Not provided

Quick links

Citations

6 review citations

Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides.
Bhattacharjya et al. (2022)
5 more

2 mentions without citation

Structural Plasticity of LL-37 Indicates Elaborate Functional Adaptation Mechanisms to Bacterial Target Structures.
Zeth et al. (2021)
1 more