3usn

Solution NMR

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE THIADIAZOLE INHIBITOR IPNU-107859, NMR, 1 STRUCTURE

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:

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: 168 amino acids
Theoretical weight: 18.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-267; Coverage: 37%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: RESTRAINED ENERGY MINIMIZATION AND RESTRAINED MOLECULAR DYNAMICS
Expression system: Escherichia coli