Solution NMR

solution structure of matrix metalloproteinase 3 (MMP-3) in the presence of n-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4-sulfonamide] hydroxamic acid (MLC88)


Function and Biology Details

Reaction catalysed:
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P08254 (Residues: 105-265; Coverage: 35%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 15%
Refinement method: molecular dynamics
Chemical shifts: BMR15395  
Expression system: Escherichia coli BL21(DE3)