PDBe 2ddf

X-ray diffraction
1.7Å resolution

Crystal structure of TACE in complex with TAPI-2

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Disintegrin and metalloproteinase domain-containing protein 17 Chains: A, B
Molecule details ›
Chains: A, B
Length: 257 amino acids
Theoretical weight: 29.01 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P78536 (Residues: 218-474; Coverage: 32%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 74.394Å b: 75.639Å c: 103.713Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.23
Expression system: Trichoplusia ni