› 2d1o

X-ray diffraction
2.02Å resolution

Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor

Released:
DOI: 10.2210/pdb2d1o/pdb
PDB entry 2d1o coloured by chain, front view.
PDB entry 2d1o coloured by chain, side view.
PDB entry 2d1o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453.
Kohno T, Hochigai H, Yamashita E, Tsukihara T, Kanaoka M
Biochem Biophys Res Commun 344 315-22 (2006)
PMID: 16603129

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
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 19.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-270; Coverage: 37%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 6 x CA
Ligand FA4 2 x FA4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: C2
Unit cell:
a: 105.36Å b: 50.95Å c: 80.79Å
α: 90° β: 105° γ: 90°
R-values:
R R work R free
0.188 0.183 0.206
Expression system: Escherichia coli

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Citations

1 review citation

Matrix metalloproteinases in exercise and obesity.
Jaoude et al. (2016)
8 other articles

4 mentions without citation

The Main Alkaloids in Uncaria rhynchophylla and Their Anti-Alzheimer's Disease Mechanism Determined by a Network Pharmacology Approach.
Zeng et al. (2021)
3 more