1fbl

X-ray diffraction
2.5Å resolution

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-149362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Interstitial collagenase Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 42.69 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P21692 (Residues: 100-469; Coverage: 82%)
Gene name: MMP1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: I41
Unit cell:
a: 161.14Å b: 161.14Å c: 52.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 not available
Expression system: Escherichia coli