PDBe 2j0t

X-ray diffraction
2.54Å resolution

Crystal Structure of the Catalytic Domain of MMP-1 in Complex with the Inhibitory Domain of TIMP-1

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
22 kDa interstitial collagenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 170 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03956 (Residues: 101-269; Coverage: 38%)
Gene names: CLG, MMP1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 126 amino acids
Theoretical weight: 14.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P01033 (Residues: 24-149; Coverage: 69%)
Gene names: CLGI, TIMP, TIMP1
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2
Unit cell:
a: 158.098Å b: 67.85Å c: 86.241Å
α: 90° β: 100.29° γ: 90°
R-values:
R R work R free
0.249 0.248 0.275
Expression system: Escherichia coli BL21(DE3)