Research workbench
NMR structure of schistocin-1 antimicrobial peptide in presence of dpc-D38 micelles
Analyse NMR structure of schistocin-1 antimicrobial peptide in presence of dpc-D38… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M67
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Schistocin-1 antimicrobial peptide
- UniProt
- A0A5K4F504
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Schistocin-1 antimicrobial peptide | protein | 20 | 75% helix, 0% strand | A0A5K4F504 |
Ligands and binding sites
- NH2 · Amino group · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7M67 · NMR Structure of Schistocin-1 antimicrobial peptide in presence of DPC-d38 micelles · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A5K4F504
- Elsewhere: RCSB PDB 7M67 · PDBe 7M67 · UniProt A0A5K4F504
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