› 1sln

X-ray diffraction
2.27Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-702,842

Released:
DOI: 10.2210/pdb1sln/pdb
PDB entry 1sln coloured by chain, front view.
PDB entry 1sln coloured by chain, side view.
PDB entry 1sln coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD
Protein Sci 4 1966-76 (1995)
PMID: 8535233

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
UniProt:
  • Canonical: P08254 (Residues: 100-272; 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 3 x CA
Ligand 8MI 1 x 8MI
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 47.23Å b: 47.23Å c: 150.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.299
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Visse et al. (2003)
37 more

7 mentions without citation

Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.
Boon et al. (2016)
6 more