X-ray diffraction
2.5Å resolution

Structure of IL-22/IL-22R1

Source organism: Homo sapiens
Primary publication:
Structure of IL-22 bound to its high-affinity IL-22R1 chain.
Structure 16 1333-44 (2008)
PMID: 18599299

Function and Biology Details

Structure analysis Details

Assemblies composition:
Non-polymer only dimer
Non-polymer only tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Interleukin-22 Chains: L, M
Molecule details ›
Chains: L, M
Length: 141 amino acids
Theoretical weight: 16.34 KDa
Source organism: Homo sapiens
  • Canonical: Q9GZX6 (Residues: 39-67, 69-96, 98-179; Coverage: 95%)
Gene names: IL22, ILTIF, UNQ3099/PRO10096, ZCYTO18
Sequence domains: Interleukin 22 IL-10-related T-cell-derived-inducible factor
Structure domains: Growth Hormone; Chain: A;
Interleukin-22 receptor subunit alpha-1 Chains: R, S
Molecule details ›
Chains: R, S
Length: 210 amino acids
Theoretical weight: 23.96 KDa
Source organism: Homo sapiens
  • Canonical: Q8N6P7 (Residues: 17-79, 81-86, 88-88, 90-226; Coverage: 37%)
Gene names: IL22R, IL22RA1
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 54.509Å b: 75.48Å c: 101.14Å
α: 90° β: 100.89° γ: 90°
R R work R free
0.222 0.222 0.27