Research workbench
NMR structure of the antimicrobial peptide RP-1 bound to SDS micelles
Analyse NMR structure of the antimicrobial peptide RP-1 bound to SDS micelles in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RLG
- Type
- protein
- Length
- 18 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Molecule
- antimicrobial peptide RP-1
Structure
solution nmr · resolution NOT · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | antimicrobial peptide RP-1 | protein | 18 | 72% helix, 0% strand | — |
Compared structures
- 2RLG · NMR structure of the antimicrobial peptide rp-1 bound to sds 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
- Elsewhere: RCSB PDB 2RLG · PDBe 2RLG
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