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The dimeric structure of ll-37 crystallized in dpc

Analyse The dimeric structure of ll-37 crystallized in dpc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NNT
Type
protein
Length
67 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cathelicidin antimicrobial peptide
UniProt
P49913
Ligands
DPV

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACathelicidin antimicrobial peptideprotein3474% helix, 0% strandP49913
BCathelicidin antimicrobial peptideprotein3376% helix, 0% strandP49913

Ligands and binding sites

  • DPV · dodecyl 2-(trimethylammonio)ethyl phosphate · ligand · 2 copies · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 575 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5NNT · The dimeric structure of LL-37 crystallized in DPC · 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 B against A, TM-score 0.66

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