Mercury in PDB 5yc8: Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative)

The structure of Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative), PDB code: 5yc8 was solved by R.Suno, S.Maeda, S.Yasuda, K.Yamashita, K.Hirata, S.Horita, M.S.Tawaramoto, H.Tsujimoto, T.Murata, M.Kinoshita, M.Yamamoto, B.K.Kobilka, S.Iwata, T.Kobayashi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.03 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.520, 59.000, 89.220, 90.00, 98.89, 90.00
R / Rfree (%)	23.7 / 27

The binding sites of Mercury atom in the Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative) (pdb code 5yc8). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative), PDB code: 5yc8:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg502 b:71.5 occ:0.49 SG A:CYS67 2.6 43.9 1.0 O A:CYS67 3.4 38.7 1.0 O A:HOH622 3.5 39.5 1.0 CB A:CYS67 3.8 44.6 1.0 CA A:CYS67 3.9 41.9 1.0 CG1 A:ILE71 4.0 38.0 1.0 C A:CYS67 4.0 40.8 1.0 CD1 A:ILE71 4.1 40.5 1.0 HG A:HG503 4.2 89.5 0.3 CE A:MET45 4.3 35.9 1.0 CD2 A:LEU70 4.5 37.3 1.0 CB A:LEU70 4.7 36.3 1.0 SD A:MET45 4.9 34.0 0.7 CG A:LEU70 5.0 35.5 1.0

Mercury binding site 2 out of 3 in the Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg503 b:89.5 occ:0.28 SG A:CYS67 2.7 43.9 1.0 CH2 A:TRP148 2.7 40.3 1.0 CZ2 A:TRP148 2.8 41.8 1.0 CZ3 A:TRP148 3.4 38.8 1.0 CD1 A:ILE71 3.5 40.5 1.0 CE2 A:TRP148 3.5 42.1 1.0 CB A:CYS67 3.9 44.6 1.0 CE3 A:TRP148 4.0 39.0 1.0 CD2 A:TRP148 4.1 40.7 1.0 C A:CYS67 4.1 40.8 1.0 O A:CYS67 4.2 38.7 1.0 HG A:HG502 4.2 71.5 0.5 N A:ALA68 4.3 33.8 1.0 NE1 A:TRP148 4.4 43.4 1.0 CA A:ALA68 4.5 33.1 1.0 CG1 A:ILE71 4.6 38.0 1.0 CA A:CYS67 4.7 41.9 1.0 O A:HOH622 5.0 39.5 1.0

Mercury binding site 3 out of 3 in the Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Crystal Structure of Rationally Thermostabilized M2 Muscarinic Acetylcholine Receptor Bound with Nms (Hg-Derivative) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg504 b:57.7 occ:0.69 SG A:CYS439 2.6 58.0 1.0 O A:ILE435 3.0 38.7 1.0 N A:CYS439 3.5 61.5 1.0 CA A:CYS439 3.6 61.9 1.0 CB A:CYS439 3.7 60.5 1.0 C A:ALA438 3.8 38.5 1.0 C A:ILE435 4.1 37.4 1.0 O A:ALA438 4.1 39.8 1.0 CB A:ALA438 4.1 38.4 1.0 CB A:ILE435 4.2 36.0 1.0 CG1 A:ILE435 4.4 34.0 1.0 CA A:ALA438 4.5 38.9 1.0 CA A:ILE435 4.7 36.9 1.0 CD1 A:ILE435 4.7 33.5 1.0 CB A:ALA395 4.8 26.1 1.0 N A:ALA438 5.0 37.8 1.0

R.Suno, S.Lee, S.Maeda, S.Yasuda, K.Yamashita, K.Hirata, S.Horita, M.S.Tawaramoto, H.Tsujimoto, T.Murata, M.Kinoshita, M.Yamamoto, B.K.Kobilka, N.Vaidehi, S.Iwata, T.Kobayashi. Structural Insights Into the Subtype-Selective Antagonist Binding to the M2MUSCARINIC Receptor Nat. Chem. Biol. V. 14 1150 2018.
ISSN: ESSN 1552-4469
PubMed: 30420692
DOI: 10.1038/S41589-018-0152-Y