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Structure of il-18 ser mutant I

Analyse Structure of il-18 ser mutant I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4XFS
Type
protein
Length
313 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin-18
UniProt
Q14116
Pockets
3 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-18protein1568% helix, 53% strandQ14116
BInterleukin-18protein1578% helix, 52% strandQ14116

Ligands and binding sites

  • DMS · Dimethyl sulfoxide · additive · 5 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14240.630.7750empty
21830.460.7530empty
31030.420.7714empty

Interfaces

1 interface between chains.

  • A–B · 486 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 4XFS · Structure of IL-18 SER Mutant I · the same entry in another collection · chain A against A, TM-score 1.00
  • Q14116 · AlphaFold monomer V2.0 prediction for interleukin-18 (Q14116) · a predicted model of the same protein · chain A against A, TM-score 0.98

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