3dpf

X-ray diffraction
2.1Å resolution

Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor

Released:

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, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 18.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22894 (Residues: 100-262; Coverage: 37%)
Gene names: CLG1, MMP8
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 68.3Å b: 69.21Å c: 81.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.27
Expression system: Escherichia coli