› 1usn

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-142372

Released:
DOI: 10.2210/pdb1usn/pdb
PDB entry 1usn coloured by chain, front view.
PDB entry 1usn coloured by chain, side view.
PDB entry 1usn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.
Finzel BC, Baldwin ET, Bryant GL, Hess GF, Wilks JW, Trepod CM, Mott JE, Marshall VP, Petzold GL, Poorman RA, O'Sullivan TJ, Schostarez HJ, Mitchell MA
Protein Sci 7 2118-26 (1998)
PMID: 9792098

Function and Biology Details

Reaction catalysed: 
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-140079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P08254 (Residues: 100-264; Coverage: 36%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 3 x ZN
Ligand CA 3 x CA
Ligand IN9 1 x IN9
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: R32
Unit cell:
a: 72.12Å b: 72.12Å c: 192.06Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

The design of inhibitors for medicinally relevant metalloproteins.
Jacobsen et al. (2007)
2 more

4 mentions without citation

A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity.
Lukacova et al. (2005)
3 more