PDBe 1cgl

X-ray diffraction
2.4Å resolution

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

Released:

Function and Biology Details

Reaction catalysed:
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
22 kDa interstitial collagenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 169 amino acids
Theoretical weight: 18.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P03956 (Residues: 101-269; Coverage: 38%)
Gene names: CLG, MMP1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P64
Unit cell:
a: 78.2Å b: 78.2Å c: 87.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Escherichia coli BL21(DE3)