1t3g

X-ray diffraction
2.3Å resolution

Crystal structure of the Toll/interleukin-1 receptor (TIR) domain of human IL-1RAPL

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL.
J Biol Chem 279 31664-70 (2004)
PMID: 15123616

Function and Biology Details

Reaction catalysed:
(1a) NAD(+) = cyclic ADP-ribose + nicotinamide
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interleukin-1 receptor accessory protein-like 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 19.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZN1 (Residues: 403-561; Coverage: 24%)
Gene names: IL1RAPL1, OPHN4
Sequence domains: TIR domain
Structure domains: Toll/interleukin-1 receptor homology (TIR) domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 51.987Å b: 53.265Å c: 183.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.272
Expression system: Escherichia coli