› 7kp8

X-ray diffraction
3.15Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-279537 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor necrosis factor, soluble form Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 147 amino acids
Theoretical weight: 16.32 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P06804 (Residues: 89-235; Coverage: 63%)
Gene names: Tnf, Tnfa, Tnfsf2
Sequence domains: TNF(Tumour Necrosis Factor) family
Tumor necrosis factor-binding protein 1 Chains: E, F
Molecule details ›
Chains: E, F
Length: 142 amino acids
Theoretical weight: 16.05 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P19438 (Residues: 43-184; Coverage: 33%)
Gene names: TNFAR, TNFR1, TNFRSF1A
Sequence domains: TNFR/NGFR cysteine-rich region

Ligands and Environments

1 bound ligand:
Ligand A7G 1 x A7G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P41212
Unit cell:
a: 133.577Å b: 133.577Å c: 141.445Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.272
Expression systems:
  • Escherichia coli
  • unidentified baculovirus

Quick links

Citations

5 review citations

Mapping, Structure and Modulation of PPI.
Martino et al. (2021)
4 more

4 mentions without citation

Structural insights into the disruption of TNF-TNFR1 signalling by small molecules stabilising a distorted TNF.
McMillan et al. (2021)
3 more