Research workbench
Gramicidin cscl complex
Analyse Gramicidin cscl complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C4D
- Type
- protein
- Length
- 64 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- BREVIBACILLUS BREVIS
- Molecule
- Gramicidin a
- Ligands
- CS, CL
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 0% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Gramicidin a | protein | 16 | 0% helix, 69% strand | — |
Ligands and binding sites
- CS · Cesium ion · metal · 8 copies · chains A, B, C, D
- CL · Chloride ion · ion · 6 copies · chains A, B, C, D
- MOH · Methanol · additive · 13 copies · chains A, B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- C–D · 1264 Ų buried · 51 hydrogen bonds · protein-protein
- A–B · 1262 Ų buried · 46 hydrogen bonds · protein-protein
- A–C · 137 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 127 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 79 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 d-amino, 8 modified (D-amino acid, nonstandard).
Compared structures
- 1C4D · Gramicidin cscl complex · the same entry in another collection · chain A against A, TM-score 0.94
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1C4D · PDBe 1C4D
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