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

Source organism: Homo sapiens
Biochemical function: zinc ion binding
Biological process: proteolysis
Cellular component: extracellular matrix

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EC 3.4.24.65: Macrophage elastase

Reaction catalysed:
Hydrolysis of soluble and insoluble elastin (1). Specific cleavages are also produced at -Ala(14)-|-Leu- and -Tyr(16)-|-Leu- in the B chain of insulin (2).
Systematic name:
-
Alternative Name(s):
  • Human macrophage metalloelastase (HME)
  • Matrix metalloproteinase 12
  • Metalloelastase

GO terms

Biochemical function:
Biological process:
Cellular component:

Sequence family

Pfam Protein family (Pfam)
PF00413
Domain description: Matrixin
Occurring in:
  1. Macrophage metalloelastase
The deposited structure of PDB entry 4h30 contains 2 copies of Pfam domain PF00413 (Matrixin) in Macrophage metalloelastase. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR021190
Domain description: Peptidase M10A
Occurring in:
  1. Macrophage metalloelastase
IPR033739
Domain description: Peptidase M10A, catalytic domain
Occurring in:
  1. Macrophage metalloelastase
IPR001818
Domain description: Peptidase M10, metallopeptidase
Occurring in:
  1. Macrophage metalloelastase
IPR024079
Domain description: Metallopeptidase, catalytic domain superfamily
Occurring in:
  1. Macrophage metalloelastase
IPR006026
Domain description: Peptidase, metallopeptidase
Occurring in:
  1. Macrophage metalloelastase

Structure domain

CATH CATH domain
3.40.390.10
Class: Alpha Beta
Architecture: 3-Layer(aba) Sandwich
Topology: Collagenase (Catalytic Domain)
Homology: Collagenase (Catalytic Domain)
Occurring in:
  1. Macrophage metalloelastase
The deposited structure of PDB entry 4h30 contains 2 copies of CATH domain 3.40.390.10 (Collagenase (Catalytic Domain)) in Macrophage metalloelastase. Showing 1 copy in chain A.

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