PDBe 3shi

X-ray diffraction
2.2Å resolution

Crystal structure of human MMP1 catalytic domain at 2.2 A resolution

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, G, M
Molecule details ›
Chains: A, G, M
Length: 156 amino acids
Theoretical weight: 17.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03956 (Residues: 106-261; Coverage: 35%)
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
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2
Unit cell:
a: 147.694Å b: 54.528Å c: 94.905Å
α: 90° β: 120.69° γ: 90°
R-values:
R R work R free
0.215 0.209 0.278
Expression system: Escherichia coli