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Membrane-bound dimer structure of protegrin-1 (pg-1), a beta-hairpin antimicrobial peptide in lipid bilayers from rotational-echo double- resonance solid-state NMR
Analyse Membrane-bound dimer structure of protegrin-1 (pg-1), a beta-hairpin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZY6
- Type
- protein
- Length
- 36 residues
- Chains
- 2
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protegrin 1
- UniProt
- P32194
- Ligands
- NH2
Structure
solid-state nmr · 1 distinct chain · 0% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protegrin 1 | protein | 18 | 0% helix, 56% strand | P32194 |
Ligands and binding sites
- NH2 · Amino group · ion · 2 copies · 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 · 210 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1ZY6 · Membrane-bound dimer structure of Protegrin-1 (PG-1), a beta-Hairpin Antimicrobial… · the same entry in another collection · chain A against A, TM-score 1.00
- P32194 · AlphaFold monomer V2.0 prediction for protegrin-1 (P32194) · a predicted model of the same protein · chain A against A, TM-score 0.34
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 P32194
- Elsewhere: RCSB PDB 1ZY6 · PDBe 1ZY6 · UniProt P32194
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