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Crystal structure of human il-18 in complex with ectromelia virus il- 18 binding protein

Analyse Crystal structure of human il-18 in complex with ectromelia virus il- 18… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3F62
Type
protein
Length
253 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin 18 binding protein; Interleukin-18
UniProt
Q9IW12, Q14116
Pockets
1 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin 18 binding proteinprotein1083% helix, 53% strandQ9IW12
BInterleukin-18protein1456% helix, 54% strandQ14116

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11090.400.7619empty

Interfaces

1 interface between chains.

  • A–B · 992 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3F62 · Crystal Structure of Human IL-18 in complex with Ectromelia virus IL-18 Binding Protein · 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 B against A, TM-score 0.96

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