X-ray diffraction
2.36Å resolution

catalytic domain of stromelysin-1 in complex with N-Hydroxy-2-(4-methoxy-N-(pyridine-3-ylmethyl)phenylsulfonamido)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: 167 amino acids
Theoretical weight: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P08254 (Residues: 100-266; Coverage: 36%)
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: 56.964Å b: 120.512Å c: 46.627Å
α: 90° β: 90° γ: 90°
R R work R free
0.262 0.261 0.283
Expression system: Escherichia coli BL21(DE3)