Seminal Fluid Protein PDC-109 (Domain B)
CYS 102;HIS 403;HIS 407;HIS 413(catalytic Zinc)
;HIS 201;HIS 205;HIS 211(catalytic Zinc)
CYS 73;HIS 374;HIS 378;HIS 384(catalytic Zinc)
Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.
The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function.
X-ray structure of gelatinase a catalytic domain complexed with a hydroxamate inhibitor.
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct.
Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14.
Specific collagenolysis by gelatinase A, MMP-2, is determined by the hemopexin domain and not the fibronectin-like domain.
Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.
Endostatin binds to the catalytic domain of matrix metalloproteinase-2.
Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2.
Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor.
Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2).
Selective hydrolysis of triple-helical substrates by matrix metalloproteinase-2 and -9.
Distinct roles of catalytic and pexin-like domains in membrane-type matrix metalloproteinase (MMP)-mediated pro-MMP-2 activation and collagenolysis.
This enzyme belongs to the peptidase family M10A. Although the catalytic residue and catalytic zinc are annotated, the detailed catalytic mechanism is still unclear.