EC Number   |
|---|
    3.1.1.1 | - |
| 3.1.1.1 | alignment studies show that enzyme has an alpha/beta hydrolase fold with catalytic triad formed by S190, E305, and H394 |
| 3.1.1.1 | at 2.0 and 1.58 A resolution. Enzyme folds into a catalytic domain, an alpha/beta domain and a regulatory domain. Residue C408 adjacent to the active site is triply oxidized and may have a regulatory role |
| 3.1.1.1 | at 2.1 A resolution. Enzyme exhibits a classical alpha/beta hydrolase fold with a central parallel-stranded beta sheet surrounded by alpha helices on both sides. The catalytic motif is formed by residues S154, D251, and H281. Enzyme forms a dimer via hydrophobic interactions through residues V274 and F276 on the beta strand off each monomer, and via salt bridges |
| 3.1.1.1 | carboxylesterase 1 in complex with cyclosarin, sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.3 M Li2SO4, 0.1 M citrate, pH 5.5, 0.1 M NaCl, 0.1 M LiCl, and 5% (v/v) glycerol. |
| 3.1.1.1 | covalent acyl-enzyme intermediate complexes of isoform hCE1 with inhibitors soman and tabun. Enzyme binds stereoselectively, (S)-stereoisomer of soman is preferred 10000fold over the (R)-isomer. Comparison with similar complexes of acetylcholinesterase |
| 3.1.1.1 | crystal structure of hCE1 in complex with the cocaine analogue homatropine to 2.8 A resolution, and with the heroin analogue naloxone to 2.9 A resolution |
| 3.1.1.1 | crystallized in the presence of either 10 mM naloxone methiodide or 100 mM homatropine using sitting drop vapor diffusion at 22°C. Overview of hCE1 structures, crystal structures of the hCE1 glycoprotein in complex with the cocaine analog homatropine and the heroin analog naloxone provide details about narcotic metabolism in humans. The hCE1 active site contains both specific and promiscuous compartments, which enable the enzyme to act on structurally distinct chemicals. A selective surface ligand-binding site regulates the trimer-hexamer equilibrium of hCE1 and allows each hCE1 monomer to bind two narcotic molecules simultaneously |
| 3.1.1.1 | crystals diffract to 2.8 A and belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 A |
| 3.1.1.1 | double-mutant M211S/R215L with bound inhibitor 1-hexadecanesulfonyl chloride, hanging drop vapour diffusion method, equal volumes of protein-inhibitor solution and reservoir solution, the latter containing 2 M ammonium sulfate, 0.1 M Tris buffer, pH 8.5, 2 weeks, X-ray diffraction structure determination and analysis at 2.3 A resolution |
