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

Analyse Crystal structure of the gorilla LL37(17-29) antimicrobial peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6S6N
Type
protein
Length
26 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cathelicidin antimicrobial peptide
UniProt
Q1KLY3

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCathelicidin antimicrobial peptideprotein1385% helix, 0% strandQ1KLY3

Interfaces

1 interface between chains.

  • A–B · 179 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6S6N · Crystal structure of the Gorilla LL37(17-29) antimicrobial peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q1KLY3 · AlphaFold monomer V2.0 prediction for cathelicidin antimicrobial peptide (Q1KLY3) · a predicted model of the same protein · chain B against A, TM-score 0.82

Analyse

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