› 1ks0

Solution NMR

The First Fibronectin Type II Module from Human Matrix Metalloproteinase 2

Released:
DOI: 10.2210/pdb1ks0/pdb
PDB entry 1ks0 coloured by chain, ensemble of 50 models, front view.
PDB entry 1ks0 coloured by chain, ensemble of 50 models, side view.
PDB entry 1ks0 coloured by chain, ensemble of 50 models, top view.
Source organism: Homo sapiens
Primary publication:
The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains.
Gehrmann M, Briknarová K, Bányai L, Patthy L, Llinás M
Biol Chem 383 137-48 (2002)
PMID: 11928808

Function and Biology Details

Reaction catalysed: 
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140074 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
72 kDa type IV collagenase Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 7.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08253 (Residues: 223-282; Coverage: 10%)
Gene names: CLG4A, MMP2
Sequence domains:
Structure domains: Fibronectin, type II, collagen-binding

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing/molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Gelatinase-mediated migration and invasion of cancer cells.
Björklund et al. (2005)
3 more

4 mentions without citation

Protein structure similarity from Principle Component Correlation analysis.
Zhou et al. (2006)
3 more