Structure analysis

Crystal structure of a mutated catalytic domain of Human MMP12 in complex with RXP470

X-ray diffraction
1.303Å 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: 8000 Å2
Buried surface area: 1600 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Interface energy (ΔGint): -60 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 159 amino acids
Theoretical weight: 17.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)

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