PDBe 3f17

X-ray diffraction
1.1Å resolution

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-(2-nitroso-2-oxoethyl)biphenyl-4-sulfonamide


Function and Biology Details

Reaction catalysed:
Hydrolysis of soluble and insoluble elastin (1). Specific cleavages are also produced at -Ala(14)-|-Leu- and -Tyr(16)-|-Leu- in the B chain of insulin (2).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macrophage metalloelastase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: NEW P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 51.636Å b: 60.25Å c: 54.22Å
α: 90° β: 115.44° γ: 90°
R R work R free
0.171 0.17 0.181
Expression system: Escherichia coli