› 2oxu

X-ray diffraction
1.24Å resolution

Uninhibited form of human MMP-12

Released:
DOI: 10.2210/pdb2oxu/pdb
PDB entry 2oxu coloured by chain, front view.
PDB entry 2oxu coloured by chain, side view.
PDB entry 2oxu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Snapshots of the reaction mechanism of matrix metalloproteinases.
Bertini I, Calderone V, Fragai M, Luchinat C, Maletta M, Yeo KJ
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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 51.545Å b: 60.751Å c: 54.264Å
α: 90° β: 115.64° γ: 90°
R-values:
R R work R free
0.198 0.197 0.216
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Architecture and function of metallopeptidase catalytic domains.
Cerdà-Costa et al. (2014)
7 more

9 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
8 more