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Atomic resolution structure of ll-37 in a monomeric state

Analyse Atomic resolution structure of ll-37 in a monomeric state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NMN
Type
protein
Length
34 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cathelicidin antimicrobial peptide
UniProt
P49913
Ligands
NA

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACathelicidin antimicrobial peptideprotein3485% helix, 0% strandP49913

Ligands and binding sites

  • NA · Sodium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 5NMN · Atomic resolution structure of LL-37 in a monomeric state · the same entry in another collection · chain A against A, TM-score 1.00
  • P49913 · AlphaFold monomer V2.0 prediction for cathelicidin antimicrobial peptide (P49913) · a predicted model of the same protein · chain A against A, TM-score 0.67

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