› 1umt

Solution NMR

Stromelysin-1 catalytic domain with hydrophobic inhibitor bound, ph 7.0, 32oc, 20 mm cacl2, 15% acetonitrile; nmr average of 20 structures minimized with restraints

Released:
DOI: 10.2210/pdb1umt/pdb
PDB entry 1umt coloured by chain, front view.
PDB entry 1umt coloured by chain, side view.
PDB entry 1umt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.
Van Doren SR, Kurochkin AV, Hu W, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER
Protein Sci 4 2487-98 (1995)
PMID: 8580839

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 Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 19.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-273; Coverage: 38%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand 0DS 1 x 0DS
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Insights into MMP-TIMP interactions.
Bode et al. (1999)
4 more

1 mention without citation

A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity.
Lukacova et al. (2005)