Research workbench
NMR structure of HSP1-NH2 antimicrobial peptide in presence of dpc-D38 micelles
Analyse NMR structure of HSP1-NH2 antimicrobial peptide in presence of dpc-D38 micelles in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WPD
- Type
- protein
- Length
- 14 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HSP1-NH2
- UniProt
- P84292
- Ligands
- NH2
Structure
solution nmr · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HSP1-NH2 | protein | 14 | 79% helix, 0% strand | P84292 |
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
- 6WPD · NMR Structure of HSP1-NH2 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 P84292
- Elsewhere: RCSB PDB 6WPD · PDBe 6WPD · UniProt P84292
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