2oi0

X-ray diffraction
2Å resolution

Crystal structure analysis 0f the TNF-a Coverting Enzyme (TACE) in complexed with Aryl-sulfonamide

Released:

Function and Biology Details

Reaction catalysed:
Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disintegrin and metalloproteinase domain-containing protein 17 Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 30.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P78536 (Residues: 216-477; Coverage: 33%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12B Reprolysin-like
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 56.55Å b: 50.06Å c: 42.98Å
α: 90° β: 92.58° γ: 90°
R-values:
R R work R free
0.213 0.21 0.268
Expression system: Not provided