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:
Model geometry
Fit model/data
Data not deposited

Function and Biology Details

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

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:
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