Research workbench
The structure of the human tetrameric ll-37 peptide in a channel conformation
Analyse The structure of the human tetrameric ll-37 peptide in a channel conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PDC
- Type
- protein
- Length
- 57 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathelicidin antimicrobial peptide
- UniProt
- P49913
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathelicidin antimicrobial peptide | protein | 30 | 90% helix, 0% strand | P49913 |
| B | Cathelicidin antimicrobial peptide | protein | 27 | 93% helix, 0% strand | P49913 |
Ligands and binding sites
- CL · Chloride ion · ion · 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 · 447 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 7PDC · The structure of the human tetrameric LL-37 peptide in a channel conformation · 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 0.72
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P49913
- Elsewhere: RCSB PDB 7PDC · PDBe 7PDC · UniProt P49913
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.