› 4gql

X-ray diffraction
1.15Å resolution

Crystal structure of the catalytic domain of Human MMP12 in complex with selective phosphinic inhibitor RXP470.1

Released:
DOI: 10.2210/pdb4gql/pdb
PDB entry 4gql coloured by chain, front view.
PDB entry 4gql coloured by chain, side view.
PDB entry 4gql coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular determinants of a selective matrix metalloprotease-12 inhibitor: insights from crystallography and thermodynamic studies.
Czarny B, Stura EA, Devel L, Vera L, Cassar-Lajeunesse E, Beau F, Calderone V, Fragai M, Luchinat C, Dive V
J Med Chem 56 1149-59 (2013)
PMID: 23343195

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-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
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 R47 1 x R47
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 69.58Å b: 63.39Å c: 36.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.134 0.133 0.154
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Matrix metalloproteinases as breast cancer drivers and therapeutic targets.
Radisky et al. (2015)
5 more

3 mentions without citation

Role of metalloproteases in the CD95 signaling pathways.
Devel et al. (2022)
2 more