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Crystal structure of a parallel six-helix coiled coil cc-TYPE2-vv

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

PDB
6G65
Type
protein
Length
360 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cc-TYPE2-vv
Ligands
ACE, NH2
Pockets
2 · best druggability 0.69

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, LCc-TYPE2-vvprotein3093% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
  • NH2 · Amino group · ion · 12 copies · chains A, D, B, E, C, F, G, J, H, K, I, L

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15930.690.7860NH2, ACE
26740.690.7764ACE

Interfaces

24 interfaces between chains.

  • B–C · 778 Ų buried · 2 hydrogen bonds · protein-protein
  • J–K · 759 Ų buried · 4 hydrogen bonds · protein-protein
  • D–E · 757 Ų buried · 2 hydrogen bonds · protein-protein
  • K–L · 748 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 744 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 covalent (covalent ligand).

Compared structures

  • 6G65 · Crystal structure of a parallel six-helix coiled coil CC-Type2-VV · the same entry in another collection · chain A against A, TM-score 1.00

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