› 1hfs

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THE N-CARBOXY-ALKYL INHIBITOR L-764,004

Released:
DOI: 10.2210/pdb1hfs/pdb
PDB entry 1hfs coloured by chain, front view.
PDB entry 1hfs coloured by chain, side view.
PDB entry 1hfs coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibition of stromelysin-1 (MMP-3) by P1'-biphenylylethyl carboxyalkyl dipeptides.
Esser CK, Bugianesi RL, Caldwell CG, Chapman KT, Durette PL, Girotra NN, Kopka IE, Lanza TJ, Levorse DA, MacCoss M, Owens KA, Ponpipom MM, Simeone JP, Harrison RK, Niedzwiecki L, Becker JW, Marcy AI, Axel MG, Christen AJ, McDonnell J, Moore VL, Olszewski JM, Saphos C, Visco DM, Hagmann WK
J Med Chem 40 1026-40 (1997)
PMID: 9083493

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 105-264; Coverage: 35%)
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 L04 1 x L04
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 84.14Å b: 85.35Å c: 55.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.217
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

4 mentions without citation

Structural signatures of enzyme binding pockets from order-independent surface alignment: a study of metalloendopeptidase and NAD binding proteins.
Dundas et al. (2011)
3 more