› 1qia

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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 162 amino acids
Theoretical weight: 18.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 106-267; 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: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P1
Unit cell:
a: 55.2Å b: 57.63Å c: 73.19Å
α: 99.25° β: 109.82° γ: 89.93°
R-values:
R R work R free
0.19 0.19 0.24
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

POVME: an algorithm for measuring binding-pocket volumes.
Durrant et al. (2011)
4 more