Controlling the self-assembly of synthetic metal-coordinating coiled- coil peptides: orthorhombic lattice from a trimeric coiled coil

Structure

x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 6 copies · chains A, B, C, D, E, F
• CU · Copper (II) ion · metal · 6 copies · chains A, B, C, D, E, F
• NH2 · Amino group · ion · 6 copies · chains A, B, C, D, E, F
• CL · Chloride ion · ion · 6 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

9 interfaces between chains.

• D–F · 536 Ų buried · 1 hydrogen bond · protein-protein
• B–C · 529 Ų buried · 2 hydrogen bonds · protein-protein
• A–C · 528 Ų buried · 1 hydrogen bond · protein-protein
• E–F · 521 Ų buried · 1 hydrogen bond · protein-protein
• D–E · 517 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 covalent, 6 modified (covalent ligand, nonstandard).

Compared structures

• 6OLN · Controlling the Self-Assembly of Synthetic Metal-Coordinating Coiled-Coil Peptides… · 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 6OLN · PDBe 6OLN