Fluorine in PDB 2dqz: Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate

All present enzymatic activity of Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate:
3.1.1.1;

The structure of Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate, PDB code: 2dqz was solved by S.Bencharit, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.60 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.564, 181.017, 202.560, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.4

The binding sites of Fluorine atom in the Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate (pdb code 2dqz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate, PDB code: 2dqz:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate within 5.0Å range: probe atom residue distance (Å) B Occ A:F4002 b:23.3 occ:1.00 N A:GLY1143 2.4 23.4 1.0 OG A:SER1221 2.6 22.5 1.0 N A:GLY1142 2.7 26.1 1.0 N A:ALA1222 2.9 23.1 1.0 CB A:SER1221 3.1 20.6 1.0 CB A:ALA1222 3.1 24.7 1.0 CA A:GLY1142 3.3 24.2 1.0 C A:GLY1142 3.3 24.1 1.0 CA A:GLY1143 3.3 24.2 1.0 C3 A:PLM111 3.4 63.1 1.0 CA A:ALA1222 3.6 23.0 1.0 C A:GLY1141 3.8 26.0 1.0 O2 A:PLM111 3.8 61.2 1.0 C A:SER1221 3.9 21.7 1.0 CA A:GLY1141 4.0 25.2 1.0 C2 A:PLM111 4.1 61.9 1.0 CA A:SER1221 4.1 20.2 1.0 C1 A:PLM111 4.2 61.9 1.0 C5 A:PLM111 4.3 66.1 1.0 C4 A:PLM111 4.4 63.0 1.0 O A:GLY1142 4.5 23.4 1.0 C A:GLY1143 4.6 24.8 1.0 N A:LEU1144 4.7 24.3 1.0 C A:ALA1222 4.8 22.3 1.0 O A:HOH7047 4.8 17.5 1.0 O A:GLU1220 4.9 21.3 1.0 O A:GLY1141 4.9 27.2 1.0 O A:SER1221 4.9 21.9 1.0 N A:GLY1223 5.0 19.9 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate within 5.0Å range: probe atom residue distance (Å) B Occ B:F4001 b:15.9 occ:1.00 OG B:SER2221 2.4 19.9 1.0 N B:ALA2222 2.6 23.5 1.0 N B:GLY2143 2.6 26.3 1.0 CB B:SER2221 2.9 21.8 1.0 N B:GLY2142 3.0 21.8 1.0 CB B:ALA2222 3.1 23.4 1.0 CA B:ALA2222 3.3 23.8 1.0 CA B:GLY2143 3.4 27.6 1.0 O1 B:PLM112 3.4 63.4 1.0 C2 B:PLM112 3.4 64.0 1.0 C1 B:PLM112 3.6 63.8 1.0 C B:SER2221 3.6 23.2 1.0 C B:GLY2142 3.6 25.5 1.0 CA B:GLY2142 3.7 23.2 1.0 CA B:SER2221 3.8 23.2 1.0 C B:GLY2141 4.0 19.9 1.0 CA B:GLY2141 4.0 19.1 1.0 O2 B:PLM112 4.4 64.0 1.0 C3 B:PLM112 4.5 63.8 1.0 C5 B:PLM112 4.5 66.2 1.0 C B:ALA2222 4.6 23.8 1.0 C B:GLY2143 4.6 29.6 1.0 O B:SER2221 4.7 23.0 1.0 O B:GLY2142 4.8 26.8 1.0 O B:GLU2220 4.8 26.1 1.0 N B:GLY2223 4.8 23.1 1.0 N B:LEU2144 4.8 29.1 1.0 C4 B:PLM112 4.9 65.8 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human Carboxylesterase in Complex with Homatropine, Coenzyme A, and Palmitate within 5.0Å range: probe atom residue distance (Å) B Occ C:F4003 b:35.7 occ:1.00 OG C:SER3221 2.4 22.6 1.0 N C:GLY3143 2.7 16.2 1.0 N C:GLY3142 2.7 18.6 1.0 N C:ALA3222 2.7 21.9 1.0 CB C:SER3221 2.9 23.2 1.0 CB C:ALA3222 3.2 21.2 1.0 CA C:GLY3142 3.4 15.2 1.0 C C:GLY3142 3.5 16.1 1.0 CA C:ALA3222 3.5 20.8 1.0 O5P C:COA1 3.6 67.6 1.0 CA C:GLY3143 3.7 15.4 1.0 C C:SER3221 3.7 22.2 1.0 C C:GLY3141 3.7 20.4 1.0 CA C:GLY3141 3.8 20.6 1.0 CA C:SER3221 3.9 22.2 1.0 C5P C:COA1 4.2 68.3 1.0 S1P C:COA1 4.2 69.3 1.0 N4P C:COA1 4.3 67.5 1.0 C2P C:COA1 4.4 69.3 1.0 O C:GLU3220 4.6 24.0 1.0 O C:GLY3142 4.7 17.4 1.0 C C:ALA3222 4.8 20.2 1.0 O C:HOH7079 4.8 9.5 1.0 O C:SER3221 4.8 23.8 1.0 O C:GLY3141 4.8 19.7 1.0 C C:GLY3143 4.8 16.6 1.0 N C:GLY3223 4.9 18.5 1.0 N C:LEU3144 4.9 18.0 1.0

S.Bencharit, C.C.Edwards, C.L.Morton, E.L.Howard-Williams, P.Kuhn, P.M.Potter, M.R.Redinbo. Multisite Promiscuity in the Processing of Endogenous Substrates By Human Carboxylesterase 1 J.Mol.Biol. V. 363 201 2006.
ISSN: ISSN 0022-2836
PubMed: 16962139
DOI: 10.1016/J.JMB.2006.08.025