› 1kbc

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil collagenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22894 (Residues: 99-262; Coverage: 37%)
Gene names: CLG1, MMP8
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

4 bound ligands:
Ligand CA 4 x CA
Ligand ZN 4 x ZN
Ligand HLE 2 x HLE
Ligand RIN 2 x RIN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.7Å b: 80.8Å c: 108.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 not available
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting.
Gialeli et al. (2011)
13 more

4 mentions without citation

Towards third generation matrix metalloproteinase inhibitors for cancer therapy.
Overall et al. (2006)
3 more