› 1ft4

X-ray diffraction
2.9Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor necrosis factor-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 162 amino acids
Theoretical weight: 18.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19438 (Residues: 41-201; Coverage: 38%)
Gene names: TNFAR, TNFR1, TNFRSF1A
Structure domains: Tumor Necrosis Factor Receptor, subunit A, domain 2

Ligands and Environments

1 bound ligand:
Ligand 703 1 x 703
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P41212
Unit cell:
a: 67.8Å b: 67.8Å c: 190Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.275 0.274 not available
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Therapeutic potential of TNFα inhibitors in chronic inflammatory disorders: Past and future.
Zhang et al. (2021)
13 more

3 mentions without citation

Photochemically enhanced binding of small molecules to the tumor necrosis factor receptor-1 inhibits the binding of TNF-alpha.
Carter et al. (2001)
2 more