X-ray diffraction
2.67Å resolution

Crystal structure of the active form (full-length) of human fibroblast collagenase.

Source organism: Homo sapiens
Primary publication:
Crystal structure of an active form of human MMP-1.
J. Mol. Biol. 362 78-88 (2006)
PMID: 16890240

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
Interstitial collagenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 42.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P03956 (Residues: 100-466; Coverage: 82%)
Gene names: CLG, MMP1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P3221
Unit cell:
a: 138.485Å b: 138.485Å c: 110.046Å
α: 90° β: 90° γ: 120°
R R work R free
0.223 0.223 0.259
Expression system: Escherichia coli BL21(DE3)