2d1o

X-ray diffraction
2.02Å resolution

Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 19.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-270; Coverage: 37%)
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: MACSCIENCE
Spacegroup: C2
Unit cell:
a: 105.36Å b: 50.95Å c: 80.79Å
α: 90° β: 105° γ: 90°
R-values:
R R work R free
0.188 0.183 0.206
Expression system: Escherichia coli