PDBe 1su3

X-ray diffraction
2.2Å resolution

X-ray structure of human proMMP-1: New insights into collagenase action

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:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo octamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interstitial collagenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 450 amino acids
Theoretical weight: 51.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03956 (Residues: 20-469; Coverage: 100%)
Gene names: CLG, MMP1
Sequence domains:
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: I422
Unit cell:
a: 142.746Å b: 142.746Å c: 295.308Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.223 0.252
Expression system: Escherichia coli BL21(DE3)