1bqo

X-ray diffraction
2.3Å resolution

DISCOVERY OF POTENT, ACHIRAL MATRIX METALLOPROTEINASE INHIBITORS

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

Assemblies composition:
homo dimer (preferred)
homo trimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 173 amino acids
Theoretical weight: 19.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-272; Coverage: 38%)
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: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 37.9Å b: 79Å c: 106.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.294
Expression system: Escherichia coli