PDBe 3ma2

X-ray diffraction
2.05Å resolution

Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase-1 (TIMP-1)

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

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14 Chains: A, D
Molecule details ›
Chains: A, D
Length: 181 amino acids
Theoretical weight: 20.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: NEW P50281 (Residues: 112-292; Coverage: 32%)
Gene name: MMP14
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1 Chains: B, C
Molecule details ›
Chains: B, C
Length: 125 amino acids
Theoretical weight: 14.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: NEW P01033 (Residues: 24-148; Coverage: 68%)
Gene names: CLGI, TIMP, TIMP1
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 59.69Å b: 63.649Å c: 87.158Å
α: 90° β: 105.86° γ: 90°
R-values:
R R work R free
0.199 0.196 0.247
Expression system: Escherichia coli BL21