PDBe 2fv5

X-ray diffraction
2.1Å resolution

Crystal structure of TACE in complex with IK682

Released:
Source organism: Homo sapiens
Primary publication:
IK682, a tight binding inhibitor of TACE.
Arch. Biochem. Biophys. 451 43-50 (2006)
PMID: 16762314

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: 261 amino acids
Theoretical weight: 29.38 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P78536 (Residues: 216-475; Coverage: 32%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 74.614Å b: 75.696Å c: 103.258Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.256
Expression system: Trichoplusia ni