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Periplasmic coiled coil domain of the fapf amyloid transporter

Analyse Periplasmic coiled coil domain of the fapf amyloid transporter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FUE
Type
protein
Length
223 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fapf
UniProt
C4IN73
Ligands
ZN, NA
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 90% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CFapfprotein3887% helix, 0% strandC4IN73
DFapfprotein3694% helix, 0% strandC4IN73
EFapfprotein3692% helix, 0% strandC4IN73
FFapfprotein3789% helix, 0% strandC4IN73

Ligands and binding sites

  • ZN · Zinc ion · metal · 11 copies · chains A, D, B, E, C, F
  • NA · Sodium ion · metal · 6 copies · chains B, D, F
  • IPA · Isopropyl alcohol · additive · chains 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16670.710.7848empty

Interfaces

9 interfaces between chains.

  • A–C · 788 Ų buried · 7 hydrogen bonds · protein-protein
  • D–E · 783 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 770 Ų buried · 5 hydrogen bonds · protein-protein
  • E–F · 745 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 712 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 6FUE · Periplasmic coiled coil domain of the FapF amyloid transporter · the same entry in another collection · chain A against A, TM-score 1.00

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