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The yfib-yfir complex

Analyse The yfib-yfir complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EB1
Type
protein
Length
543 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Yfir; Yfib
UniProt
Q9I4L4, Q9I4L6
Ligands
SO4
Pockets
5 · best druggability 0.60

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AYfirprotein14733% helix, 25% strandQ9I4L4
B, DYfibprotein12444% helix, 15% strandQ9I4L6
CYfirprotein14832% helix, 25% strandQ9I4L4

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains B, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12050.600.8129empty
22110.590.8124empty
3890.350.7518empty
4830.350.7518empty
5540.270.7414empty

Interfaces

3 interfaces between chains.

  • C–D · 1645 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 1641 Ų buried · 17 hydrogen bonds · protein-protein
  • A–C · 633 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5EB1 · the YfiB-YfiR complex · the same entry in another collection · chain A against A, TM-score 1.00

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