PDBe 3c7x

X-ray diffraction
1.7Å resolution

Hemopexin-like domain of matrix metalloproteinase 14

Released:

Function and Biology Details

Reaction catalysed:
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Matrix metalloproteinase-14 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 23.13 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P50281 (Residues: 316-511; Coverage: 35%)
Gene name: MMP14
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3121
Unit cell:
a: 77.21Å b: 77.21Å c: 66.819Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.185 0.207
Expression system: Homo sapiens