Function and Biology

Crystal structure of an MMP twin carboxylate based inhibitor LC20 in complex with the MMP-9 catalytic domain

Source organism: Homo sapiens
Biochemical function: metallopeptidase activity
Biological process: leukocyte migration
Cellular component: extracellular matrix

EC 3.4.24.35: Gelatinase B

Reaction catalysed:
Cleavage of gelatin types I and V and collagen types IV and V.
Comments:
  • Belongs to peptidase family M10B.
Systematic name:
-
Alternative Name(s):
  • 92-kDa gelatinase
  • 92-kDa type IV collagenase
  • 95 kDa type IV collagenase/gelatinase
  • MMP 9
  • Collagenase IV
  • Collagenase type IV
  • Gelatinase MMP 9
  • Macrophage gelatinase
  • Matrix metalloproteinase 9
  • Type IV collagen metalloproteinase
  • Type V collagenase

Sequence family

CATH InterPro annotations
IPR021190
Domain description: Peptidase M10A
Occurring in:
  1. 67 kDa matrix metalloproteinase-9
IPR033739
Domain description: Peptidase M10A, catalytic domain
Occurring in:
  1. 67 kDa matrix metalloproteinase-9
IPR001818
Domain description: Peptidase M10, metallopeptidase
Occurring in:
  1. 67 kDa matrix metalloproteinase-9
IPR006026
Domain description: Peptidase, metallopeptidase
Occurring in:
  1. 67 kDa matrix metalloproteinase-9
IPR028688
Domain description: Matrix metalloproteinase-9
Occurring in:
  1. 67 kDa matrix metalloproteinase-9
IPR024079
Domain description: Metallopeptidase, catalytic domain
Occurring in:
  1. 67 kDa matrix metalloproteinase-9