› 1jj9

X-ray diffraction
2Å resolution

Crystal Structure of MMP8-Barbiturate Complex Reveals Mechanism for Collagen Substrate Recognition

Released:
DOI: 10.2210/pdb1jj9/pdb
PDB entry 1jj9 coloured by chain, front view.
PDB entry 1jj9 coloured by chain, side view.
PDB entry 1jj9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition.
Brandstetter H, Grams F, Glitz D, Lang A, Huber R, Bode W, Krell HW, Engh RA
J Biol Chem 276 17405-12 (2001)
PMID: 11278347

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: 163 amino acids
Theoretical weight: 18.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P22894 (Residues: 100-262; Coverage: 37%)
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 BBT 1 x BBT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I222
Unit cell:
a: 61.02Å b: 69.23Å c: 88.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.296
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Anthocyanins and their role in cancer prevention.
Wang et al. (2008)
14 more

2 mentions without citation

A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity.
Lukacova et al. (2005)
1 more