Mercury in PDB 2j4f: Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative

All present enzymatic activity of Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative:
3.1.1.7;

The structure of Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative, PDB code: 2j4f was solved by D.I.Kreimer, E.A.Dolginova, M.Raves, J.L.Sussman, I.Silman, L.Weiner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.0 / 2.8
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	110.700, 110.700, 135.000, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 26.2

The binding sites of Mercury atom in the Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative (pdb code 2j4f). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative, PDB code: 2j4f:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1536 b:44.0 occ:0.45 ND1 A:HIS471 1.7 30.9 1.0 CE1 A:HIS471 2.4 33.4 1.0 OE2 A:GLU139 2.4 29.2 1.0 OE1 A:GLU139 2.7 25.7 1.0 CG A:HIS471 2.9 31.8 1.0 CD A:GLU139 2.9 25.9 1.0 O A:HOH2088 3.3 37.1 1.0 NE2 A:HIS471 3.5 35.2 1.0 CB A:HIS471 3.6 30.4 1.0 CD2 A:HIS471 3.8 32.9 1.0 CA A:HIS471 4.2 28.0 1.0 CG A:GLU139 4.4 23.1 1.0 O A:THR138 4.7 23.4 1.0 O A:HOH2089 4.9 18.2 1.0

Mercury binding site 2 out of 2 in the Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Torpedo Acetylcholinesterase - Hg Heavy-Atom Derivative within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1537 b:30.4 occ:0.65 N A:SER228 2.3 12.3 1.0 SG A:CYS231 2.3 24.5 1.0 O A:SER228 2.3 19.4 1.0 OG A:SER228 2.4 15.3 1.0 C A:GLY227 3.0 12.4 1.0 CA A:SER228 3.0 14.0 1.0 C A:SER228 3.0 15.1 1.0 CB A:SER228 3.2 11.2 1.0 CB A:CYS231 3.2 18.2 1.0 CA A:GLY227 3.3 11.5 1.0 O A:GLY227 3.9 13.7 1.0 CZ2 A:TRP233 4.1 13.6 1.0 CA A:CYS231 4.2 17.2 1.0 N A:CYS231 4.2 17.5 1.0 N A:PRO229 4.3 14.2 1.0 N A:GLY227 4.4 10.5 1.0 CB A:ALA204 4.6 12.8 1.0 CB A:PRO403 4.7 10.1 1.0 O A:ASN399 4.7 16.6 1.0 OD1 A:ASN230 4.7 5.2 1.0 CE2 A:TRP233 4.7 13.0 1.0 CH2 A:TRP233 4.8 12.5 1.0 O A:VAL400 4.9 16.6 1.0 O A:SER226 4.9 13.6 1.0 NE1 A:TRP233 5.0 14.4 1.0

D.I.Kreimer, E.A.Dolginova, M.Raves, J.L.Sussman, I.Silman, L.Weiner. A Metastable State of Torpedo Californica Acetylcholinesterase Generated By Modification with Organomercurials Biochemistry V. 33 14407 1994.
ISSN: ISSN 0006-2960
PubMed: 7981200
DOI: 10.1021/BI00252A006