Research workbench
Gramicidin a in hydrated dmpc bilayers, solid state NMR
Analyse Gramicidin a in hydrated dmpc bilayers, solid state NMR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MAG
- Type
- protein
- Length
- 30 residues
- Chains
- 2
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gramicidin a
- Ligands
- ETA
Structure
solid-state nmr · 1 distinct chain · 0% helix, 87% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Gramicidin a | protein | 15 | 0% helix, 87% strand | — |
Ligands and binding sites
- ETA · Ethanolamine · ligand · 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 · 211 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 d-amino, 2 covalent, 2 modified (D-amino acid, covalent ligand, nonstandard).
Compared structures
- 1MAG · Gramicidin a in hydrated dmpc bilayers, solid state NMR · the same entry in another collection · chain B against B, 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 1MAG · PDBe 1MAG
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