Matrix Metalloproteinase 12: Difference between revisions

The <scene name='User:Julie_Frentzel/Sandbox_1/Active_site/1'>active site of the enzyme</scene> is composed by one Glu residue near 3 His residues which maintain a <scene name='User:Julie_Frentzel/Sandbox_1/Zinc_et_eau/1'>Zn2+ atom coordinated with three water molecules</scene>. One of them is as well bound to the Glu residue thanks to a hydrogen bond. The second Zn2+ atom is not involved in the active site. At first, the Gly 206 residue of the substrate binds the active site thanks to the Zn2+ atom. When it binds it takes the place of unstable water molecules and establishes stabilizing interactions with the active site thanks to its C terminal part. Then, the <scene name='User:Julie_Frentzel/Sandbox_1/J/1'>Ala 182</scene> residue of the enzyme makes a hydrogen bond with the NH group of the substrate:  this allows the substrate to enter the cavity of the catalytic site.