› 1a85

X-ray diffraction
2Å resolution

MMP8 WITH MALONIC AND ASPARAGINE BASED INHIBITOR

Released:
DOI: 10.2210/pdb1a85/pdb
PDB entry 1a85 coloured by chain, front view.
PDB entry 1a85 coloured by chain, side view.
PDB entry 1a85 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F
Protein Sci 7 1303-9 (1998)
PMID: 9655333

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:
Sequence domains:
Structure domain:

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: 158 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P22894 (Residues: 105-262; Coverage: 35%)
Gene names: CLG1, MMP8
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand ZN 2 x ZN
Ligand 0DY 1 x 0DY
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 33.14Å b: 69.43Å c: 72.62Å
α: 90° β: 90° γ: 90°

Quick links

Citations

3 review citations

Structural aspects of the metzincin clan of metalloendopeptidases.
Gomis-Rüth FX. (2003)
2 more

5 mentions without citation

Coupling protein engineering with probe design to inhibit and image matrix metalloproteinases with controlled specificity.
Morell et al. (2013)
4 more