2oxw

X-ray diffraction
1.15Å resolution

Human MMP-12 complexed with the peptide IAG

Released:
Source organism: Homo sapiens
Primary publication:
Snapshots of the reaction mechanism of matrix metalloproteinases.
Angew Chem Int Ed Engl 45 7952-5 (2006)
PMID: 17096442

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-153973 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Macrophage metalloelastase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
ILE-ALA-GLY peptide Chain: X
Molecule details ›
Chain: X
Length: 3 amino acids
Theoretical weight: 259 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 51.888Å b: 60.358Å c: 54.521Å
α: 90° β: 115.73° γ: 90°
R-values:
R R work R free
0.199 0.197 0.222
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided