Structure analysis

Crystal structure of the catalytic domain of MMP-12 in complex with a twin inhibitor.

X-ray diffraction
2.16Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 14800 Å2
Buried surface area: 4700 Å2
Dissociation area: 900 Å2
Dissociation energy (ΔGdiss): 12 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -130 kcal/mol
Symmetry number: 2
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 14800 Å2
Buried surface area: 3700 Å2
Dissociation area: 850 Å2
Dissociation energy (ΔGdiss): 14 kcal/mol
Dissociation entropy (TΔSdiss): 12 kcal/mol
Interface energy (ΔGint): -141 kcal/mol
Symmetry number: 2

Macromolecules

Chains: A, B, C, D
Length: 159 amino acids
Theoretical weight: 17.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Pfam: Matrixin
InterPro:

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