2oy4

X-ray diffraction
1.7Å resolution

Uninhibited human MMP-8

Released:
DOI:
Source organism: Homo sapiens
Primary publication:
Snapshots of the reaction mechanism of matrix metalloproteinases.
Angew Chem Int Ed Engl 45 7952-5 (2006)
PMID: 17096442

Function and Biology Details

Reaction catalysed:
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neutrophil collagenase Chains: A, F
Molecule details ›
Chains: A, F
Length: 158 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22894 (Residues: 105-262; Coverage: 35%)
Gene names: CLG1, MMP8
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: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 33.294Å b: 47.11Å c: 61.325Å
α: 77.73° β: 80.04° γ: 77.01°
R-values:
R R work R free
0.231 0.225 0.293
Expression system: Escherichia coli BL21(DE3)