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 (preferred)
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Multimeric state: monomeric
Accessible surface area: 8500 Å2
Buried surface area: 1700 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -84 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 8100 Å2
Buried surface area: 1800 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -75 kcal/mol
Symmetry number: 1

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
InterPro:

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