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

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

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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