GL1X · GenesisL1 explorer

MolNFT v1 · #149644 · protein

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

6G6G: “Crystal structure of a parallel six-helix coiled coil cc-TYPE2-fi”. X-ray diffraction, 2 ligands (ACE, NH2), 1 pocket (best druggability 0.65). MolNFT v1 #149644 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6G6G
Type
protein
Length
360 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cc-TYPE2-fi
Ligands
ACE, NH2
Pockets
1 · best druggability 0.65

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-fiprotein3093% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 11 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
  • NH2 · Amino group · ion · 4 copies · chains B, C, D, I

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14170.650.7840empty

Interfaces

24 interfaces between chains.

  • J–K · 841 Ų buried · 3 hydrogen bonds · protein-protein
  • K–L · 829 Ų buried · 6 hydrogen bonds · protein-protein
  • D–E · 818 Ų buried · 2 hydrogen bonds · protein-protein
  • H–I · 800 Ų buried · 4 hydrogen bonds · protein-protein
  • G–H · 797 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 6G6G · Crystal structure of a parallel six-helix coiled coil CC-Type2-FI · the same entry in another collection · chain A against A, TM-score 1.00

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