Structure analysis

Crystal structure of TACE in complex with IK682

X-ray diffraction
2.1Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 12569.11 Å2
Buried surface area: 1045.98 Å2
Dissociation area: 486.16 Å2
Dissociation energy (ΔGdiss): 7.78 kcal/mol
Dissociation entropy (TΔSdiss): 5.1 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-160275
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 12321.49 Å2
Buried surface area: 1054.05 Å2
Dissociation area: 489.86 Å2
Dissociation energy (ΔGdiss): 8.22 kcal/mol
Dissociation entropy (TΔSdiss): 5.09 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-160275

Macromolecules

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
Pfam: Metallo-peptidase family M12B Reprolysin-like
InterPro:
CATH: Collagenase (Catalytic Domain)

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