› 1bm6

Solution NMR

SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 COMPLEXED TO A POTENT NON-PEPTIDIC INHIBITOR, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1bm6/pdb
PDB entry 1bm6 coloured by chain, ensemble of 20 models, front view.
PDB entry 1bm6 coloured by chain, ensemble of 20 models, side view.
PDB entry 1bm6 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor.
Li YC, Zhang X, Melton R, Ganu V, Gonnella NC
Biochemistry 37 14048-56 (1998)
PMID: 9760240

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: 173 amino acids
Theoretical weight: 19.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08254 (Residues: 100-272; Coverage: 38%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

5 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 2 x CA
Ligand HAV 1 x HAV
Ligand 3MP 1 x 3MP
Ligand MSB 1 x MSB
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs.
Cuniasse et al. (2005)
1 more

6 mentions without citation

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