› 1ums

Solution NMR

STROMELYSIN-1 CATALYTIC DOMAIN WITH HYDROPHOBIC INHIBITOR BOUND, PH 7.0, 32OC, 20 MM CACL2, 15% ACETONITRILE; NMR ENSEMBLE OF 20 STRUCTURES

Released:
DOI: 10.2210/pdb1ums/pdb
PDB entry 1ums coloured by chain, ensemble of 20 models, front view.
PDB entry 1ums coloured by chain, ensemble of 20 models, side view.
PDB entry 1ums coloured by chain, ensemble of 20 models, 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

2 mentions without citation

Conformational variability of matrix metalloproteinases: beyond a single 3D structure.
Bertini et al. (2005)
1 more