PDBe 1hfs

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-764,004

Released:

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

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 105-264; Coverage: 35%)
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
Spacegroup: C2221
Unit cell:
a: 84.14Å b: 85.35Å c: 55.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.217
Expression system: Escherichia coli