Mercury in PDB 1gze: Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant)

The structure of Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant), PDB code: 1gze was solved by J.Menetrey, G.Flatau, E.A.Stura, J.B.Charbonnier, F.Gas, J.M.Teulon, M.H.Le Du, P.Boquet, A.Menez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.12 / 2.7
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.997, 75.596, 123.465, 90.00, 102.37, 90.00
R / Rfree (%)	24 / 29

The binding sites of Mercury atom in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant) (pdb code 1gze). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant), PDB code: 1gze:
Jump to Mercury binding site number: 1; 2; 3; 4;

Mercury binding site 1 out of 4 in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg1248 b:62.6 occ:1.00 SG A:CYS177 2.1 40.9 1.0 SD A:MET215 2.7 44.4 1.0 CB A:CYS177 3.0 45.5 1.0 CE2 A:PHE49 3.3 70.0 1.0 CE A:MET215 3.3 44.5 1.0 CD2 A:PHE49 3.5 69.7 1.0 CA A:CYS177 3.6 44.9 1.0 CZ3 A:TRP58 3.8 50.5 1.0 CD2 A:LEU126 4.0 47.2 1.0 CE3 A:TRP58 4.3 51.7 1.0 CZ A:PHE49 4.4 69.8 1.0 CH2 A:TRP58 4.4 51.1 1.0 CG A:MET215 4.5 43.9 1.0 N A:CYS177 4.5 44.5 1.0 C A:CYS177 4.7 46.5 1.0 CG A:PHE49 4.8 68.0 1.0 O A:CYS177 4.8 45.5 1.0 CD1 A:TYR202 4.9 57.7 1.0

Mercury binding site 2 out of 4 in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg1247 b:81.6 occ:1.00 SG B:CYS177 2.3 46.5 1.0 CB B:CYS177 3.1 48.8 1.0 CE2 B:PHE49 3.4 66.7 1.0 SD B:MET215 3.4 40.4 1.0 CA B:CYS177 3.5 50.0 1.0 CD2 B:PHE49 3.6 66.6 1.0 CZ3 B:TRP58 4.0 51.3 1.0 CE3 B:TRP58 4.2 52.5 1.0 CG B:MET215 4.3 38.0 1.0 CD2 B:LEU126 4.4 46.6 1.0 N B:CYS177 4.4 49.5 1.0 CZ B:PHE49 4.5 66.3 1.0 CD1 B:ILE124 4.7 51.1 1.0 C B:CYS177 4.7 51.4 1.0 CG B:PHE49 4.8 65.8 1.0 O B:CYS177 4.8 50.4 1.0 CH2 B:TRP58 4.9 51.6 1.0

Mercury binding site 3 out of 4 in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg1252 b:71.6 occ:1.00 SG C:CYS177 2.4 40.8 1.0 CB C:CYS177 3.0 48.7 1.0 SD C:MET215 3.3 52.4 1.0 CE C:MET215 3.4 48.3 1.0 CA C:CYS177 3.5 49.1 1.0 CE2 C:PHE49 3.7 64.1 1.0 CZ3 C:TRP58 3.9 33.0 1.0 CD2 C:PHE49 4.0 65.2 1.0 N C:CYS177 4.3 47.6 1.0 CE3 C:TRP58 4.3 34.2 1.0 CD2 C:LEU126 4.4 51.9 1.0 C C:CYS177 4.7 52.1 1.0 CH2 C:TRP58 4.7 34.5 1.0 O C:CYS177 4.8 51.7 1.0 CZ C:PHE49 4.9 64.2 1.0 CG C:MET215 5.0 46.4 1.0

Mercury binding site 4 out of 4 in the Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Structure of the Clostridium Botulinum C3 Exoenzyme (L177C Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ D:Hg1247 b:59.5 occ:1.00 SG D:CYS177 2.3 41.0 1.0 CB D:CYS177 2.9 42.9 1.0 CE2 D:PHE49 3.4 49.9 1.0 CD2 D:PHE49 3.4 51.2 1.0 CA D:CYS177 3.5 42.9 1.0 SD D:MET215 3.9 46.1 1.0 CZ3 D:TRP58 3.9 37.9 1.0 CE3 D:TRP58 4.0 36.7 1.0 N D:CYS177 4.3 43.5 1.0 CE D:MET215 4.4 43.0 1.0 CD2 D:LEU126 4.4 44.8 1.0 CZ D:PHE49 4.7 49.8 1.0 CG D:PHE49 4.7 50.8 1.0 C D:CYS177 4.7 43.9 1.0 CH2 D:TRP58 4.8 38.7 1.0 CD2 D:TRP58 4.9 37.9 1.0 O D:CYS177 4.9 44.7 1.0

J.Menetrey, G.Flatau, E.A.Stura, J.B.Charbonnier, F.Gas, J.M.Teulon, M.H.Le Du, P.Boquet, A.Menez. Nad Binding Induces Conformational Changes in Rho Adp-Ribosylating Clostridium Botulinum C3 Exoenzyme J.Biol.Chem. V. 277 30950 2002.
ISSN: ISSN 0021-9258
PubMed: 12029083
DOI: 10.1074/JBC.M201844200