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Crystal structure of catalytic domain of TACE with tartrate-based inhibitor

Source organism: Homo sapiens
Biochemical function: metallopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

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EC 3.4.24.86: ADAM 17 endopeptidase

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.
Systematic name:
-
Alternative Name(s):
  • TACE
  • Tumor necrosis factor alpha-converting enzyme

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF13574
Domain description: Metallo-peptidase family M12B Reprolysin-like
Occurring in:
  1. Disintegrin and metalloproteinase domain-containing protein 17

InterPro InterPro annotations
IPR034025
Domain description: ADAM10/ADAM17 catalytic domain
Occurring in:
  1. Disintegrin and metalloproteinase domain-containing protein 17
IPR001590
Domain description: Peptidase M12B, ADAM/reprolysin
Occurring in:
  1. Disintegrin and metalloproteinase domain-containing protein 17
IPR024079
Domain description: Metallopeptidase, catalytic domain superfamily
Occurring in:
  1. Disintegrin and metalloproteinase domain-containing protein 17

Structure domain

CATH CATH domain
3.40.390.10
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Collagenase (Catalytic Domain)
Homology: Collagenase (Catalytic Domain)
Occurring in:
  1. Disintegrin and metalloproteinase domain-containing protein 17
The deposited structure of PDB entry 3kmc contains 2 copies of CATH domain 3.40.390.10 (Collagenase (Catalytic Domain)) in Disintegrin and metalloproteinase domain-containing protein 17. Showing 1 copy in chain A.

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