Mercury in PDB 4acb: Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp

The structure of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp, PDB code: 4acb was solved by M.Leibundgut, C.Frick, M.Thanbichler, A.Boeck, N.Ban, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.938 / 3.34
Space group	P 31 1 2
Cell size a, b, c (Å), α, β, γ (°)	146.630, 146.630, 297.220, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 22.33

The structure of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 16;

Binding sites:

The binding sites of Mercury atom in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp (pdb code 4acb). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 16 binding sites of Mercury where determined in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp, PDB code: 4acb:
Jump to Mercury binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Mercury binding site 1 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


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 Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg264 b:0.2 occ:0.58 HG A:CMH264 0.0 0.2 0.6 CM A:CMH264 2.1 0.0 0.6 SG A:CMH264 2.3 0.0 1.0 N A:CMH264 2.9 0.9 1.0 CA A:CMH264 3.1 0.6 1.0 C A:GLY263 3.1 0.3 1.0 CB A:CMH264 3.2 0.2 1.0 CZ A:TYR261 3.3 1.0 1.0 CE2 A:TYR261 3.4 0.2 1.0 CD A:PRO222 3.5 0.5 1.0 CE1 A:TYR261 3.6 1.0 1.0 O A:GLY263 3.6 0.5 1.0 OH A:TYR261 3.7 0.6 1.0 CA A:GLY263 3.8 0.4 1.0 CD2 A:TYR261 3.8 0.5 1.0 N A:GLY263 3.9 0.7 1.0 O A:LEU221 3.9 0.5 1.0 CD1 A:TYR261 4.0 0.7 1.0 CG A:TYR261 4.1 0.8 1.0 O A:TYR261 4.1 0.2 1.0 CG A:PRO222 4.4 0.6 1.0 N A:TYR261 4.5 0.5 1.0 N A:PRO222 4.5 0.4 1.0 C A:TYR261 4.5 0.6 1.0 C A:CMH264 4.6 0.8 1.0 C A:LEU221 4.6 0.5 1.0 CA A:TYR261 4.9 0.5 1.0 C A:ARG262 5.0 0.1 1.0

Mercury binding site 2 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


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 Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg338 b:0.4 occ:0.28 HG A:CMH338 0.0 0.4 0.3 CM A:CMH338 2.1 0.6 0.3 SG A:CMH338 2.3 0.1 1.0 O A:GLU337 2.9 0.5 1.0 C A:GLU337 2.9 0.7 1.0 N A:CMH338 3.1 0.5 1.0 CB A:CMH338 3.2 0.3 1.0 N A:GLU337 3.4 0.5 1.0 CA A:CMH338 3.4 0.9 1.0 O A:GLY335 3.7 0.9 1.0 CA A:GLU337 3.8 0.5 1.0 CG2 A:ILE333 3.8 0.6 1.0 CA A:ILE333 4.1 0.7 1.0 CD2 A:LEU329 4.2 0.0 1.0 O A:ILE333 4.3 0.6 1.0 C A:ASN336 4.4 1.0 1.0 O A:VAL332 4.4 0.6 1.0 C A:ILE333 4.4 0.3 1.0 CB A:ILE333 4.6 0.1 1.0 CA A:ASN336 4.6 0.3 1.0 CD1 A:LEU329 4.6 0.1 1.0 C A:GLY335 4.7 0.2 1.0 CB A:GLU337 4.8 0.2 1.0 C A:CMH338 4.9 0.7 1.0 CG A:LEU329 4.9 0.3 1.0

Mercury binding site 3 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


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 Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg340 b:0.9 occ:0.83 HG A:CMH340 0.0 0.9 0.8 CM A:CMH340 2.1 1.0 0.8 SG A:CMH340 2.3 0.9 1.0 CD1 A:ILE283 3.1 1.0 1.0 CB A:CMH340 3.1 0.8 1.0 OH A:TYR291 3.5 0.9 1.0 O A:CMH338 3.8 0.8 1.0 CB A:PRO314 3.8 0.2 1.0 CB A:ILE283 4.0 0.4 1.0 CG2 A:ILE283 4.0 0.4 1.0 CG1 A:ILE283 4.0 0.0 1.0 CA A:CMH340 4.2 0.3 1.0 CA A:PRO314 4.2 0.4 1.0 CG A:PRO314 4.3 0.6 1.0 O A:TYR339 4.4 0.1 1.0 CZ A:TYR291 4.5 0.2 1.0 CE1 A:TYR291 4.6 1.0 1.0 N A:CMH340 4.6 0.2 1.0 C A:TYR339 4.7 0.6 1.0 N A:PRO314 4.7 0.6 1.0 C A:CMH338 4.7 0.7 1.0 CB A:CMH338 4.7 0.3 1.0 CD A:PRO314 4.9 0.8 1.0

Mercury binding site 4 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 4 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg371 b:0.4 occ:0.45 HG A:CMH371 0.0 0.4 0.5 CM A:CMH371 2.1 0.2 0.5 SG A:CMH371 2.4 0.1 1.0 CB A:CMH371 3.1 1.0 1.0 CA A:CMH371 3.3 0.5 1.0 N A:CMH371 3.3 0.8 1.0 C A:ILE370 3.7 0.4 1.0 O A:ILE370 3.9 0.4 1.0 CB A:ARG360 4.2 0.2 1.0 N A:ILE370 4.5 0.1 1.0 C A:ARG369 4.6 0.9 1.0 O A:ARG369 4.7 0.9 1.0 CA A:ILE370 4.7 0.6 1.0 C A:CMH371 4.7 0.8 1.0 N A:ARG360 4.8 0.8 1.0

Mercury binding site 5 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 5 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg264 b:0.8 occ:0.83 HG B:CMH264 0.0 0.8 0.8 CM B:CMH264 2.1 73.2 0.8 SG B:CMH264 2.3 92.3 1.0 N B:CMH264 2.9 97.5 1.0 CZ B:TYR261 2.9 0.2 1.0 CE2 B:TYR261 3.0 0.3 1.0 CA B:CMH264 3.1 86.6 1.0 CB B:CMH264 3.2 76.0 1.0 C B:GLY263 3.2 0.9 1.0 CE1 B:TYR261 3.3 0.0 1.0 OH B:TYR261 3.4 0.4 1.0 CD B:PRO222 3.4 0.3 1.0 CD2 B:TYR261 3.4 0.5 1.0 O B:GLY263 3.7 99.0 1.0 CD1 B:TYR261 3.7 0.8 1.0 CG B:TYR261 3.8 0.3 1.0 N B:GLY263 3.8 0.2 1.0 CA B:GLY263 3.8 0.2 1.0 CG B:PRO222 3.9 0.7 1.0 O B:TYR261 4.1 0.1 1.0 C B:TYR261 4.3 0.2 1.0 CG1 B:ILE223 4.6 0.1 1.0 C B:ARG262 4.6 0.5 1.0 N B:TYR261 4.6 0.4 1.0 C B:CMH264 4.7 99.4 1.0 N B:ARG262 4.7 0.8 1.0 N B:PRO222 4.8 81.7 1.0 CA B:TYR261 4.8 0.9 1.0 O B:LEU221 4.8 0.2 1.0 CB B:TYR261 4.9 0.0 1.0 CD1 B:ILE223 4.9 0.8 1.0

Mercury binding site 6 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 6 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg338 b:0.7 occ:0.27 HG B:CMH338 0.0 0.7 0.3 CM B:CMH338 2.1 0.3 0.3 SG B:CMH338 2.4 0.7 1.0 C B:GLU337 3.0 0.0 1.0 O B:GLU337 3.0 1.0 1.0 N B:CMH338 3.1 0.9 1.0 CB B:CMH338 3.1 0.6 1.0 CG2 B:ILE285 3.3 0.3 1.0 CA B:CMH338 3.6 0.0 1.0 N B:GLU337 3.6 0.8 1.0 CA B:GLU337 3.8 0.6 1.0 O B:ILE283 3.8 0.1 1.0 O B:SER334 3.9 0.1 1.0 C B:ASN336 4.2 0.5 1.0 CB B:ILE285 4.3 0.3 1.0 N B:ILE285 4.3 0.1 1.0 O B:GLY335 4.6 0.4 1.0 C B:SER334 4.7 0.8 1.0 O B:ASN336 4.7 0.8 1.0 CB B:SER334 4.8 0.2 1.0 C B:GLY335 4.8 0.8 1.0 N B:ASN336 4.9 0.1 1.0 C B:CMH338 4.9 0.3 1.0 C B:ILE283 4.9 0.1 1.0 CA B:ASN336 4.9 0.5 1.0 CA B:ILE285 4.9 0.6 1.0

Mercury binding site 7 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 7 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg340 b:0.9 occ:0.90 HG B:CMH340 0.0 0.9 0.9 CM B:CMH340 2.1 0.2 0.9 SG B:CMH340 2.3 0.6 1.0 CB B:CMH340 3.1 0.1 1.0 CM B:CMH371 3.4 0.9 0.5 CE B:MET297 3.7 0.9 1.0 CG1 B:ILE283 3.7 0.3 1.0 O B:TYR339 4.0 0.3 1.0 CA B:CMH340 4.0 0.1 1.0 CB B:ILE283 4.2 0.7 1.0 CA B:PRO314 4.3 0.4 1.0 CB B:PRO314 4.3 0.8 1.0 CG2 B:ILE283 4.3 0.3 1.0 C B:TYR339 4.4 0.3 1.0 CD1 B:ILE358 4.5 0.1 1.0 N B:CMH340 4.5 0.9 1.0 N B:PRO314 4.5 0.1 1.0 O B:VAL313 4.7 0.3 1.0 CB B:CMH338 4.7 0.6 1.0 C B:VAL313 4.7 0.5 1.0 CD1 B:ILE283 4.9 0.6 1.0 CD2 B:LEU293 5.0 0.2 1.0

Mercury binding site 8 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 8 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg371 b:0.6 occ:0.50 HG B:CMH371 0.0 0.6 0.5 CM B:CMH371 2.1 0.9 0.5 SG B:CMH371 2.4 0.6 1.0 CB B:CMH371 3.2 0.2 1.0 O B:CMH371 3.7 0.7 1.0 CD1 B:ILE358 3.7 0.1 1.0 CD1 B:ILE285 3.8 0.9 1.0 C B:CMH371 3.8 0.2 1.0 CA B:CMH371 4.1 0.2 1.0 CG2 B:ILE358 4.2 0.9 1.0 N B:GLY372 4.3 0.0 1.0 CB B:ILE358 4.4 0.5 1.0 CE B:MET297 4.4 0.9 1.0 CG1 B:ILE285 4.6 0.1 1.0 CG1 B:ILE358 4.7 1.0 1.0 CA B:GLY372 4.8 0.6 1.0 N B:CMH371 5.0 0.7 1.0 CE2 B:PHE289 5.0 0.4 1.0 CM B:CMH340 5.0 0.2 0.9

Mercury binding site 9 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 9 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg264 b:0.9 occ:0.90 HG C:CMH264 0.0 0.9 0.9 CM C:CMH264 2.1 0.2 0.9 SG C:CMH264 2.3 0.3 1.0 N C:CMH264 2.9 98.7 1.0 CB C:CMH264 3.2 75.9 1.0 CA C:CMH264 3.2 70.2 1.0 CD C:PRO222 3.3 85.7 1.0 O C:TYR261 3.4 84.8 1.0 C C:GLY263 3.4 0.1 1.0 CE2 C:TYR261 3.5 0.9 1.0 CZ C:TYR261 3.6 0.3 1.0 N C:GLY263 3.7 73.5 1.0 CD2 C:TYR261 3.7 0.4 1.0 CA C:GLY263 3.8 0.5 1.0 CE1 C:TYR261 3.8 0.2 1.0 CG C:PRO222 3.9 0.4 1.0 CG C:TYR261 3.9 0.2 1.0 CD1 C:TYR261 3.9 0.6 1.0 C C:TYR261 4.0 0.1 1.0 OH C:TYR261 4.1 0.3 1.0 O C:GLY263 4.2 0.4 1.0 N C:TYR261 4.5 0.5 1.0 O C:LEU221 4.6 77.7 1.0 N C:PRO222 4.6 0.3 1.0 C C:ARG262 4.6 0.8 1.0 CA C:TYR261 4.7 0.3 1.0 C C:CMH264 4.8 0.1 1.0 N C:ARG262 4.8 0.3 1.0 CB C:TYR261 4.8 0.8 1.0

Mercury binding site 10 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 10 of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis in Complex with the Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg338 b:0.6 occ:0.70 HG C:CMH338 0.0 0.6 0.7 CM C:CMH338 2.1 0.2 0.7 SG C:CMH338 2.4 0.4 1.0 O C:GLU337 2.9 0.6 1.0 CB C:CMH338 3.4 74.2 1.0 CA C:CMH338 3.5 0.7 1.0 C C:GLU337 3.6 0.4 1.0 N C:CMH338 3.9 90.9 1.0 CB C:LYS316 4.3 0.3 1.0 N C:GLU337 4.6 0.9 1.0 CA C:GLU337 4.7 0.0 1.0 CD1 C:LEU329 4.8 89.8 1.0 C C:CMH338 4.9 87.0 1.0

M.Leibundgut, C.Frick, M.Thanbichler, A.Bock, N.Ban. Selenocysteine Trna-Specific Elongation Factor Selb Is A Structural Chimaera of Elongation and Initiation Factors. Embo J. V. 24 11 2005.
ISSN: ISSN 0261-4189
PubMed: 15616587
DOI: 10.1038/SJ.EMBOJ.7600505