1os2

X-ray diffraction
2.15Å resolution

Ternary enzyme-product-inhibitor complexes of human MMP12

Released:

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

Assemblies composition:
monomeric
homo trimer (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-153976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 165 amino acids
Theoretical weight: 18.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P39900 (Residues: 106-268; Coverage: 36%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P31
Unit cell:
a: 123.839Å b: 123.839Å c: 69.73Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.212 0.271
Expression system: Escherichia coli