1g4k

X-ray diffraction
2Å resolution

X-ray Structure of a Novel Matrix Metalloproteinase Inhibitor Complexed to Stromelysin

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, C
Molecule details ›
Chains: A, B, C
Length: 168 amino acids
Theoretical weight: 18.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-267; 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: NSLS BEAMLINE X8C
Spacegroup: P43212
Unit cell:
a: 103.8Å b: 103.8Å c: 147.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.244 0.284
Expression system: Escherichia coli