› 1biw

X-ray diffraction
2.5Å resolution

DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS

Released:
DOI: 10.2210/pdb1biw/pdb
PDB entry 1biw coloured by chain, front view.
PDB entry 1biw coloured by chain, side view.
PDB entry 1biw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of conformationally-constrained MMP inhibitors.
Natchus MG, Cheng M, Wahl CT, Pikul S, Almstead NG, Bradley RS, Taiwo YO, Mieling GE, Dunaway CM, Snider CE, McIver JM, Barnett BL, McPhail SJ, Anastasio MB, De B
Bioorg Med Chem Lett 8 2077-80 (1998)
PMID: 9873489

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 Chains: A, B
Molecule details ›
Chains: A, B
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 4 x ZN
Ligand CA 6 x CA
Ligand S80 1 x S80
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 38.06Å b: 77.28Å c: 106.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.275
Expression system: Escherichia coli

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

4 mentions without citation

A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity.
Lukacova et al. (2005)
3 more