› 3f17

X-ray diffraction
1.1Å resolution

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor N-(2-nitroso-2-oxoethyl)biphenyl-4-sulfonamide

Released:
DOI: 10.2210/pdb3f17/pdb
PDB entry 3f17 coloured by chain, front view.
PDB entry 3f17 coloured by chain, side view.
PDB entry 3f17 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinases.
Bertini I, Calderone V, Fragai M, Giachetti A, Loconte M, Luchinat C, Maletta M, Nativi C, Yeo KJ
J Am Chem Soc 129 2466-75 (2007)
PMID: 17269766

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-544352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macrophage metalloelastase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 3 x CA
Ligand HS4 1 x HS4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 51.636Å b: 60.25Å c: 54.22Å
α: 90° β: 115.44° γ: 90°
R-values:
R R work R free
0.171 0.17 0.181
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Perspectives on NMR in drug discovery: a technique comes of age.
Pellecchia et al. (2008)
10 more

11 mentions without citation

The essential protein for bacterial flagella formation FlgJ functions as a β-N-acetylglucosaminidase.
Herlihey et al. (2014)
10 more