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Crystal structure of a parallel eight-helix coiled coil cc-TYPE2-II

Analyse Crystal structure of a parallel eight-helix coiled coil cc-TYPE2-II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6G67
Type
protein
Length
60 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cc-TYPE2-II
Ligands
ACE, NH2

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCc-TYPE2-IIprotein3093% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 2 copies · chains A, B
  • NH2 · Amino group · ion · 2 copies · chains A, B
  • GOL · Glycerol · additive

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

Interfaces

1 interface between chains.

  • A–B · 791 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 6G67 · Crystal structure of a parallel eight-helix coiled coil CC-Type2-II · the same entry in another collection · chain A against A, TM-score 1.00

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