PDBe 3cki

X-ray diffraction
2.3Å resolution

Crystal structure of the TACE-N-TIMP-3 complex

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Disintegrin and metalloproteinase domain-containing protein 17 Chain: A
Molecule details ›
Chain: A
Length: 256 amino acids
Theoretical weight: 28.95 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P78536 (Residues: 219-474; Coverage: 32%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 3 Chain: B
Molecule details ›
Chain: B
Length: 121 amino acids
Theoretical weight: 13.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35625 (Residues: 24-144; Coverage: 64%)
Gene name: TIMP3
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 70.447Å b: 70.447Å c: 156.728Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.284
Expression systems:
  • Cricetulus griseus
  • Escherichia coli