PDBe 1utz

X-ray diffraction
2.5Å resolution

Crystal Structure of MMP-12 complexed to (2R)-3-({[4-[(pyridin-4-yl)phenyl]-thien-2-yl}carboxamido)(phenyl)propanoic 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:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P39900 (Residues: 106-264; Coverage: 35%)
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: RIGAKU MICROMAX-007
Spacegroup: P6322
Unit cell:
a: 123.224Å b: 123.224Å c: 168.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.245
Expression system: Escherichia coli BL21(DE3)