Mercury in PDB 1dr6: 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: 1dr6 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 (°)	88.720, 48.740, 63.870, 90.00, 124.70, 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 1dr6). 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: 1dr6:
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:Hg201 b:41.6 occ:0.65 HG A:MBO201 0.0 41.6 0.7 HG A:MBO201 1.2 39.5 0.3 CE1 A:MBO201 2.1 44.8 0.7 SG A:CYS11 2.5 24.1 0.7 O A:PHE142 2.9 38.8 1.0 N A:PHE142 2.9 31.5 1.0 SG A:CYS11 3.0 19.4 0.3 CE6 A:MBO201 3.0 47.1 0.7 CE2 A:MBO201 3.0 46.3 0.7 CA A:GLU141 3.3 41.4 1.0 CB A:CYS11 3.3 20.3 0.7 CB A:CYS11 3.3 20.1 0.3 N A:ASN13 3.5 31.5 1.0 N A:GLN12 3.5 32.6 1.0 C A:GLU141 3.5 39.6 1.0 C A:PHE142 3.8 35.8 1.0 O A:HIS140 3.9 46.5 1.0 CB A:GLU141 3.9 40.3 1.0 C A:CYS11 4.0 26.3 1.0 CA A:PHE142 4.0 28.3 1.0 CA A:CYS11 4.1 26.4 1.0 OG A:SER144 4.2 21.6 1.0 CA A:GLN12 4.2 36.8 1.0 CE5 A:MBO201 4.3 50.4 0.7 C A:GLN12 4.3 32.0 1.0 CE3 A:MBO201 4.3 47.5 0.7 CB A:ASN13 4.4 41.0 1.0 N A:GLU141 4.5 38.0 1.0 CA A:ASN13 4.5 35.8 1.0 C A:HIS140 4.6 40.4 1.0 CB A:PHE142 4.7 27.9 1.0 O A:GLU141 4.7 45.0 1.0 CB A:GLN12 4.8 44.1 1.0 O A:CYS11 4.8 33.4 1.0 CE4 A:MBO201 4.9 54.5 0.7

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:Hg201 b:39.5 occ:0.35 HG A:MBO201 0.0 39.5 0.3 HG A:MBO201 1.2 41.6 0.7 SG A:CYS11 1.8 24.1 0.7 SG A:CYS11 2.4 19.4 0.3 O A:PHE142 2.7 38.8 1.0 CE1 A:MBO201 3.0 44.8 0.7 CB A:CYS11 3.1 20.3 0.7 OG A:SER144 3.2 21.6 1.0 CB A:CYS11 3.3 20.1 0.3 N A:PHE142 3.6 31.5 1.0 N A:ASN13 3.6 31.5 1.0 CE6 A:MBO201 3.6 47.1 0.7 N A:GLN12 3.9 32.6 1.0 C A:PHE142 3.9 35.8 1.0 CA A:CYS11 3.9 26.4 1.0 C A:CYS11 3.9 26.3 1.0 CE2 A:MBO201 4.0 46.3 0.7 N A:GLY15 4.0 19.3 1.0 CB A:ASN13 4.3 41.0 1.0 CA A:GLY15 4.3 15.4 1.0 CA A:PHE142 4.3 28.3 1.0 CA A:GLU141 4.4 41.4 1.0 CA A:ASN13 4.4 35.8 1.0 CB A:SER144 4.4 15.9 1.0 C A:GLU141 4.5 39.6 1.0 N A:CYS11 4.6 26.8 1.0 C A:GLN12 4.6 32.0 1.0 O A:CYS11 4.6 33.4 1.0 CA A:GLN12 4.7 36.8 1.0 O A:GLY15 4.7 26.1 1.0 O A:HIS140 4.7 46.5 1.0 CB A:PHE142 4.8 27.9 1.0 N A:MET14 4.8 32.9 1.0 C A:GLY15 4.9 19.9 1.0 C A:ASN13 4.9 34.0 1.0 CE5 A:MBO201 5.0 50.4 0.7

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.