› 1qic

X-ray diffraction
2Å resolution

Function and Biology Details

Reaction catalysed: 
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 161 amino acids
Theoretical weight: 18.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 106-266; Coverage: 35%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand CA 12 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 71.25Å b: 59.32Å c: 72.3Å
α: 90° β: 101.64° γ: 90°
R-values:
R R work R free
0.23 0.23 0.27
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs.
Cuniasse et al. (2005)
4 more

5 mentions without citation

Chapter 4. Predicting and characterizing protein functions through matching geometric and evolutionary patterns of binding surfaces.
Liang et al. (2008)
4 more