› 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:
DOI: 10.2210/pdb1ros/pdb
PDB entry 1ros coloured by chain, front view.
PDB entry 1ros coloured by chain, side view.
PDB entry 1ros coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12.
Morales R, Perrier S, Florent JM, Beltra J, Dufour S, De Mendez I, Manceau P, Tertre A, Moreau F, Compere D, Dublanchet AC, O'Gara M
J Mol Biol 341 1063-76 (2004)
PMID: 15289103

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 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: P39900 (Residues: 106-268; Coverage: 36%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 6 x CA
Ligand DEO 2 x DEO
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)

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Citations

14 review citations

Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy.
Overall et al. (2006)
13 more

8 mentions without citation

Mechanism of cyclizing NAD to cyclic ADP-ribose by ADP-ribosyl cyclase and CD38.
Graeff et al. (2009)
7 more