› 1rmz

X-ray diffraction
1.34Å resolution

Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH at 1.3 A resolution

Released:
DOI: 10.2210/pdb1rmz/pdb
PDB entry 1rmz coloured by chain, front view.
PDB entry 1rmz coloured by chain, side view.
PDB entry 1rmz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformational variability of matrix metalloproteinases: beyond a single 3D structure.
Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P
Proc Natl Acad Sci U S A 102 5334-9 (2005)
PMID: 15809432

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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21212
Unit cell:
a: 69.194Å b: 62.564Å c: 37.262Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.215
Expression system: Escherichia coli BL21(DE3)

Quick links

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

9 mentions without citation

Zinc-binding groups modulate selective inhibition of MMPs.
Agrawal et al. (2008)
8 more