PDBe 1buv

X-ray diffraction
2.75Å resolution

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.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14 Chain: M
Molecule details ›
Chain: M
Length: 174 amino acids
Theoretical weight: 19.8 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: NEW P50281 (Residues: 114-287; Coverage: 31%)
Gene name: MMP14
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 2 Chain: T
Molecule details ›
Chain: T
Length: 184 amino acids
Theoretical weight: 20.53 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: NEW P16368 (Residues: 27-210; Coverage: 95%)
Gene name: TIMP2
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 102.65Å b: 40.1Å c: 85.68Å
α: 90° β: 102.3° γ: 90°
R-values:
R R work R free
0.189 0.189 0.248