› 1cqr

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE STROMELYSIN CATALYTIC DOMAIN AT 2.0 A RESOLUTION

Released:
DOI: 10.2210/pdb1cqr/pdb
PDB entry 1cqr coloured by chain, front view.
PDB entry 1cqr coloured by chain, side view.
PDB entry 1cqr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the stromelysin catalytic domain at 2.0 A resolution: inhibitor-induced conformational changes.
Chen L, Rydel TJ, Gu F, Dunaway CM, Pikul S, Dunham KM, Barnett BL
J Mol Biol 293 545-57 (1999)
PMID: 10543949

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
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

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 38.2Å b: 79.1Å c: 107.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.199 0.266
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The design of inhibitors for medicinally relevant metalloproteins.
Jacobsen et al. (2007)
2 more

5 mentions without citation

Structural conservation of druggable hot spots in protein-protein interfaces.
Kozakov et al. (2011)
4 more