Structure analysis

Crystal structure of mutant MMP-9 catalytic domain in complex with a twin inhibitor.

X-ray diffraction
1.59Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 8517.12 Å2
Buried surface area: 265.68 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147085
Assembly 2 (preferred)
Download    3D Visualisation
Multimeric state: monomeric
Accessible surface area: 8132.03 Å2
Buried surface area: 178.38 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147085

Macromolecules

Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14780 (Residues: 110-444; Coverage: 23%)
Gene names: CLG4B, MMP9
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)

Search similar proteins