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Crystal structure of a cc-hex mutant that forms a parallel six-helix coiled coil cc-hex*-II

Analyse Crystal structure of a cc-hex mutant that forms a parallel six-helix coiled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Q5P
Type
protein
Length
180 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cc-hex*-II
Ligands
ACE, NH2, PO4

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FCc-hex*-IIprotein3093% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 4 copies · chains A, C, D, E, F
  • NH2 · Amino group · ion · 4 copies · chains A, C, B, F
  • PO4 · Phosphate ion · ion · 2 copies · chains A, B, E, F
  • GOL · Glycerol · additive · chains B

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

Interfaces

9 interfaces between chains.

  • D–E · 690 Ų buried · 4 hydrogen bonds · protein-protein
  • E–F · 687 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 672 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 659 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 635 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 covalent (covalent ligand).

Compared structures

  • 6Q5P · Crystal structure of a CC-Hex mutant that forms a parallel six-helix coiled coil… · the same entry in another collection · chain A against A, TM-score 1.00

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