Mercury in PDB 1dr4: Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes

All present enzymatic activity of Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes:
1.5.1.3;

The structure of Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes, PDB code: 1dr4 was solved by M.A.Mctigue, J.F.Davies /Ii, B.T.Kaufman, N.-H.Xuong, J.Kraut, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.40
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.080, 48.290, 64.320, 90.00, 124.80, 90.00
R / Rfree (%)	n/a / n/a

The structure of Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Mercury atom in the Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes (pdb code 1dr4). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes, PDB code: 1dr4:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg190 b:54.5 occ:0.75 HG A:HG190 0.0 54.5 0.8 HG A:HG190 2.3 60.2 0.2 SG A:CYS11 2.4 43.9 0.8 CB A:CYS11 2.9 50.0 0.2 O A:PHE142 2.9 45.5 1.0 OD1 A:ASN13 2.9 56.4 1.0 O A:HOH705 2.9 77.9 1.0 ND2 A:ASN13 3.0 61.6 1.0 N A:PHE142 3.1 42.3 1.0 SG A:CYS11 3.1 52.4 0.2 CG A:ASN13 3.2 52.9 1.0 CB A:CYS11 3.3 37.1 0.8 CA A:GLU141 3.7 48.7 1.0 N A:ASN13 3.7 29.9 1.0 OG A:SER144 3.7 31.0 1.0 N A:GLN12 3.8 36.8 1.0 C A:PHE142 3.8 41.9 1.0 C A:GLU141 3.9 49.3 1.0 CA A:CYS11 4.0 31.0 1.0 C A:CYS11 4.0 34.0 1.0 CA A:PHE142 4.0 38.8 1.0 O A:HIS140 4.2 40.9 1.0 CB A:GLU141 4.4 53.0 1.0 CB A:ASN13 4.4 46.2 1.0 N A:GLY15 4.5 22.4 1.0 CA A:GLN12 4.5 38.5 1.0 CA A:ASN13 4.6 37.1 1.0 C A:GLN12 4.6 36.0 1.0 CB A:PHE142 4.7 34.0 1.0 N A:CYS11 4.8 28.2 1.0 O A:CYS11 4.8 35.1 1.0 N A:GLU141 4.8 44.6 1.0 CA A:GLY15 4.8 20.4 1.0 CB A:SER144 4.9 25.6 1.0 C A:HIS140 4.9 44.0 1.0 CD1 A:PHE142 4.9 35.0 1.0 CG A:GLU141 5.0 67.3 1.0

Mercury binding site 2 out of 2 in the Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg190 b:60.2 occ:0.25 HG A:HG190 0.0 60.2 0.2 SG A:CYS11 1.5 43.9 0.8 HG A:HG190 2.3 54.5 0.8 SG A:CYS11 2.5 52.4 0.2 OG A:SER144 2.5 31.0 1.0 CB A:CYS11 3.2 37.1 0.8 O A:PHE142 3.3 45.5 1.0 CB A:CYS11 3.3 50.0 0.2 O A:HOH705 3.3 77.9 1.0 O A:GLY15 3.5 22.2 1.0 CA A:GLY15 3.6 20.4 1.0 CB A:SER144 3.7 25.6 1.0 C A:GLY15 3.8 22.3 1.0 CG A:PRO23 3.8 28.6 1.0 CA A:CYS11 3.9 31.0 1.0 N A:GLY15 3.9 22.4 1.0 ND2 A:ASN13 3.9 61.6 1.0 CZ3 A:TRP24 4.0 24.1 1.0 CB A:PRO23 4.0 25.4 1.0 N A:CYS11 4.0 28.2 1.0 N A:PHE142 4.2 42.3 1.0 C A:PHE142 4.2 41.9 1.0 CB A:PHE142 4.5 34.0 1.0 CA A:PHE142 4.5 38.8 1.0 C A:CYS11 4.5 34.0 1.0 CE3 A:TRP24 4.6 30.9 1.0 CG A:ASN13 4.7 52.9 1.0 N A:ILE16 4.7 21.3 1.0 OD1 A:ASN13 4.8 56.4 1.0 CD1 A:PHE142 4.8 35.0 1.0 CA A:SER144 4.9 30.6 1.0 N A:GLN12 4.9 36.8 1.0 N A:SER144 4.9 28.7 1.0 CH2 A:TRP24 5.0 29.1 1.0

M.A.Mctigue, J.F.Davies Ii, B.T.Kaufman, N.-H.Xuong, J.Kraut. Crystal Structures of Organomercurial-Activated Chicken Liver Dihydrofolate Reductase Complexes To Be Published.