4qxu

X-ray diffraction
2.3Å resolution

Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling Conformational antibody

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-211290 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
anti_MT1-MMP Light chain Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.12 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins
anti_MT1-MMP Heavy chain Chain: H
Molecule details ›
Chain: H
Length: 231 amino acids
Theoretical weight: 25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Matrix metalloproteinase-14 Chain: K
Molecule details ›
Chain: K
Length: 11 amino acids
Theoretical weight: 1.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50281 (Residues: 218-228; Coverage: 2%)
Gene name: MMP14

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 79.56Å b: 79.56Å c: 93.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.243 0.293
Expression system: Escherichia coli