X-ray diffraction
2.5Å resolution

catalytic domain of stromelysin-1 in complex with N-Hydroxy-2-(4-methylphenylsulfonamido)acetamide

Source organism: Homo sapiens
Entry authors: Kowatz T, Naismith JH

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 dimer
Entry contents:
1 distinct polypeptide molecule
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P08254 (Residues: 100-268; Coverage: 37%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 56.482Å b: 121.044Å c: 46.872Å
α: 90° β: 90° γ: 90°
R R work R free
0.255 0.255 0.264
Expression system: Escherichia coli BL21(DE3)