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Crystal structure of the human il-17RC ecd in complex with human il- 17F

Analyse Crystal structure of the human il-17RC ecd in complex with human il- 17F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HG4
Type
protein
Length
531 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin-17F; Interleukin-17 receptor C
UniProt
Q96PD4, Q8NAC3
Pockets
5 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-17Fprotein1044% helix, 50% strandQ96PD4
BInterleukin-17 receptor Cprotein42710% helix, 48% strandQ8NAC3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17390.720.7863empty
23010.590.7734empty
3700.440.8217empty
4680.420.8012empty
5530.280.7415empty

Interfaces

1 interface between chains.

  • A–B · 1174 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 13 disulfide (disulfide).

Compared structures

  • 6HG4 · Crystal Structure of the human IL-17RC ECD in complex with human IL-17F · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8NAC3 · AlphaFold monomer V2.0 prediction for interleukin-17 receptor C (Q8NAC3) · a predicted model of the same protein · chain B against A, TM-score 0.95
  • Q96PD4 · AlphaFold monomer V2.0 prediction for interleukin-17F (Q96PD4) · a predicted model of the same protein · chain A against A, TM-score 0.92

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