3tt4

X-ray diffraction
1.88Å resolution

Human MMP8 in complex with L-glutamate motif 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 Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22894 (Residues: 104-262; Coverage: 36%)
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 ID23-1
Spacegroup: P212121
Unit cell:
a: 32.719Å b: 69.369Å c: 70.312Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.258
Expression system: Escherichia coli