PDBe 2i47

X-ray diffraction
1.9Å resolution

Crystal structure of catalytic domain of TACE with inhibitor

Released:
Source organism: Homo sapiens

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 288 amino acids
Theoretical weight: 32.59 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P78536 (Residues: 212-493; Coverage: 35%)
Gene names: ADAM17, CSVP, TACE
Sequence domains: Metallo-peptidase family M12
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 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: 61.775Å b: 126.193Å c: 81.224Å
α: 90° β: 107.41° γ: 90°
R-values:
R R work R free
0.198 0.198 0.227