PDBe 1ros

X-ray diffraction
2Å resolution

Crystal structure of MMP-12 complexed to 2-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)ethyl-4-(4-ethoxy[1,1-biphenyl]-4-yl)-4-oxobutanoic acid

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chains: A, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 18.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P39900 (Residues: 106-268; Coverage: 36%)
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: RIGAKU MICROMAX-007
Spacegroup: R3
Unit cell:
a: 123.2Å b: 123.2Å c: 59.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.199 0.239
Expression system: Escherichia coli BL21(DE3)