PDBe 1cgf

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF

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: 162 amino acids
Theoretical weight: 18.16 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P03956 (Residues: 102-263; Coverage: 36%)
Gene names: CLG, MMP1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 71Å b: 50.5Å c: 48Å
α: 90° β: 100° γ: 90°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided