Mercury in PDB 4aca: Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form

The structure of Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form, PDB code: 4aca 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)	19.971 / 3.15
Space group	P 31 1 2
Cell size a, b, c (Å), α, β, γ (°)	146.860, 146.860, 297.830, 90.00, 90.00, 120.00
R / Rfree (%)	17.25 / 21.48

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, Apo Form (pdb code 4aca). 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, Apo Form, PDB code: 4aca:
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, Apo Form


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, Apo Form 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 0.7 0.6 SG A:CMH264 2.3 0.6 1.0 N A:CMH264 2.9 0.4 1.0 CA A:CMH264 3.1 0.4 1.0 CB A:CMH264 3.2 0.3 1.0 C A:GLY263 3.2 0.2 1.0 CZ A:TYR261 3.3 0.8 1.0 CE2 A:TYR261 3.3 0.2 1.0 CD A:PRO222 3.4 0.1 1.0 CE1 A:TYR261 3.7 0.9 1.0 OH A:TYR261 3.7 0.9 1.0 CD2 A:TYR261 3.7 0.6 1.0 O A:GLY263 3.8 0.6 1.0 CA A:GLY263 3.8 0.2 1.0 N A:GLY263 3.9 0.8 1.0 CD1 A:TYR261 4.1 0.6 1.0 CG A:TYR261 4.1 0.1 1.0 O A:LEU221 4.1 0.7 1.0 CG A:PRO222 4.2 0.8 1.0 O A:TYR261 4.2 0.4 1.0 N A:TYR261 4.5 0.4 1.0 N A:PRO222 4.5 0.2 1.0 C A:CMH264 4.6 0.3 1.0 C A:TYR261 4.6 0.5 1.0 C A:LEU221 4.8 0.9 1.0 CA A:TYR261 5.0 0.4 1.0

Mercury binding site 2 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg338 b:0.2 occ:0.28 HG A:CMH338 0.0 0.2 0.3 CM A:CMH338 2.1 0.9 0.3 SG A:CMH338 2.3 0.7 1.0 CB A:CMH338 3.1 0.6 1.0 CG2 A:ILE333 3.2 0.4 1.0 O A:ASN336 3.2 0.4 1.0 O A:GLU337 3.6 0.7 1.0 C A:ASN336 3.6 0.2 1.0 C A:GLU337 3.7 0.6 1.0 N A:CMH338 3.7 0.5 1.0 CA A:CMH338 3.9 0.4 1.0 CD1 A:ILE285 4.0 0.1 1.0 O A:ILE283 4.1 0.1 1.0 N A:GLU337 4.2 0.2 1.0 O A:GLY335 4.2 0.5 1.0 CA A:ASN336 4.3 0.3 1.0 CA A:GLU337 4.4 0.2 1.0 CG1 A:ILE285 4.5 0.7 1.0 CB A:ILE333 4.5 0.3 1.0 O A:ILE333 4.6 0.8 1.0 CA A:ILE333 4.7 0.9 1.0

Mercury binding site 3 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg340 b:0.5 occ:0.88 HG A:CMH340 0.0 0.5 0.9 CM A:CMH340 2.1 0.7 0.9 SG A:CMH340 2.3 1.0 1.0 CB A:CMH340 3.2 0.9 1.0 CD1 A:ILE283 3.2 0.5 1.0 OH A:TYR291 3.6 0.6 1.0 O A:CMH338 3.9 0.5 1.0 CB A:PRO314 4.0 1.0 1.0 CG A:PRO314 4.0 0.5 1.0 CB A:ILE283 4.1 0.3 1.0 CG2 A:ILE283 4.1 0.9 1.0 CG1 A:ILE283 4.2 0.9 1.0 CA A:PRO314 4.2 0.0 1.0 CA A:CMH340 4.2 0.1 1.0 O A:TYR339 4.4 0.1 1.0 CB A:CMH338 4.4 0.6 1.0 CZ A:TYR291 4.5 0.5 1.0 N A:CMH340 4.6 0.7 1.0 CE1 A:TYR291 4.7 0.3 1.0 C A:CMH338 4.7 0.9 1.0 C A:TYR339 4.7 0.7 1.0 N A:PRO314 4.8 0.5 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, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg371 b:0.3 occ:0.40 HG A:CMH371 0.0 0.3 0.4 CM A:CMH371 2.1 0.8 0.4 SG A:CMH371 2.4 0.7 1.0 CB A:CMH371 3.1 0.8 1.0 CA A:CMH371 3.3 0.1 1.0 N A:CMH371 3.3 0.6 1.0 C A:ILE370 3.8 0.5 1.0 O A:ILE370 4.1 0.2 1.0 CB A:ARG360 4.1 0.0 1.0 C A:ARG369 4.5 0.2 1.0 O A:ARG369 4.5 0.3 1.0 N A:ILE370 4.5 0.6 1.0 CA A:ILE370 4.7 0.4 1.0 N A:ARG360 4.7 0.3 1.0 C A:CMH371 4.8 0.2 1.0

Mercury binding site 5 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg264 b:0.1 occ:0.85 HG B:CMH264 0.0 0.1 0.9 CM B:CMH264 2.1 61.2 0.8 SG B:CMH264 2.3 78.0 1.0 N B:CMH264 2.9 57.9 1.0 CZ B:TYR261 2.9 0.7 1.0 CE1 B:TYR261 3.1 0.7 1.0 CE2 B:TYR261 3.1 0.0 1.0 CA B:CMH264 3.2 67.2 1.0 CB B:CMH264 3.2 73.0 1.0 C B:GLY263 3.2 93.4 1.0 CD2 B:TYR261 3.4 0.3 1.0 CD1 B:TYR261 3.4 0.6 1.0 OH B:TYR261 3.5 0.6 1.0 CD B:PRO222 3.5 87.9 1.0 CG B:TYR261 3.6 0.5 1.0 N B:GLY263 3.7 0.9 1.0 O B:TYR261 3.7 0.3 1.0 CA B:GLY263 3.7 0.6 1.0 O B:GLY263 3.8 97.5 1.0 CG B:PRO222 3.9 92.2 1.0 C B:TYR261 4.1 95.3 1.0 N B:TYR261 4.5 86.7 1.0 CG1 B:ILE223 4.6 0.6 1.0 C B:ARG262 4.6 0.3 1.0 N B:ARG262 4.6 82.0 1.0 CA B:TYR261 4.6 90.6 1.0 CB B:TYR261 4.7 86.4 1.0 C B:CMH264 4.7 92.7 1.0 CD1 B:ILE223 4.8 0.1 1.0 N B:PRO222 4.9 74.4 1.0 O B:LEU221 4.9 0.7 1.0

Mercury binding site 6 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg338 b:0.6 occ:0.27 HG B:CMH338 0.0 0.6 0.3 CM B:CMH338 2.1 0.0 0.3 SG B:CMH338 2.4 0.5 1.0 O B:GLU337 2.9 0.2 1.0 CB B:CMH338 3.1 0.3 1.0 C B:GLU337 3.1 0.5 1.0 N B:CMH338 3.4 0.2 1.0 CG2 B:ILE285 3.7 0.8 1.0 CA B:CMH338 3.9 0.1 1.0 CA B:GLU337 3.9 0.4 1.0 O B:ILE283 4.1 0.6 1.0 CD2 B:LEU329 4.5 0.1 1.0 N B:GLU337 4.5 0.1 1.0 CB B:SER334 4.6 0.7 1.0 CB B:ILE285 4.7 0.5 1.0 CD1 B:LEU293 4.7 0.4 1.0 O B:SER334 4.7 0.9 1.0 C B:CMH338 4.8 0.1 1.0 CG2 B:ILE283 4.9 0.9 1.0 CM B:CMH340 4.9 0.1 0.9 O B:ASN336 5.0 0.9 1.0 C B:ASN336 5.0 0.6 1.0 N B:ILE285 5.0 0.2 1.0

Mercury binding site 7 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg340 b:0.1 occ:0.88 HG B:CMH340 0.0 0.1 0.9 CM B:CMH340 2.1 0.1 0.9 SG B:CMH340 2.3 0.6 1.0 CB B:CMH340 3.1 0.6 1.0 CE B:MET297 3.7 0.7 1.0 CG1 B:ILE283 3.8 0.7 1.0 CM B:CMH371 3.8 0.0 0.4 CA B:CMH340 4.0 0.8 1.0 O B:TYR339 4.0 0.7 1.0 CB B:ILE283 4.3 0.3 1.0 CG2 B:ILE283 4.3 0.9 1.0 CA B:PRO314 4.3 0.5 1.0 CD1 B:ILE358 4.3 0.2 1.0 CB B:PRO314 4.4 0.0 1.0 O B:VAL313 4.5 0.3 1.0 N B:CMH340 4.5 1.0 1.0 C B:TYR339 4.5 0.5 1.0 N B:PRO314 4.5 0.3 1.0 C B:VAL313 4.7 0.8 1.0 SG B:CMH338 4.7 0.5 1.0 CD1 B:ILE283 4.9 0.3 1.0 CZ B:PHE342 5.0 0.8 1.0 CB B:ALA312 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, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg371 b:0.1 occ:0.36 HG B:CMH371 0.0 0.1 0.4 CM B:CMH371 2.1 0.0 0.4 SG B:CMH371 2.4 0.4 1.0 CB B:CMH371 3.2 0.4 1.0 C B:CMH371 3.6 0.4 1.0 CD1 B:ILE285 3.7 0.0 1.0 CD1 B:ILE358 3.7 0.2 1.0 O B:CMH371 3.8 0.4 1.0 N B:GLY372 3.8 0.6 1.0 CA B:CMH371 4.0 0.1 1.0 CG2 B:ILE358 4.3 0.9 1.0 CA B:GLY372 4.3 0.7 1.0 CB B:ILE358 4.3 0.8 1.0 CG1 B:ILE285 4.3 0.8 1.0 CE B:MET297 4.4 0.7 1.0 CG1 B:ILE358 4.6 0.8 1.0 CM B:CMH340 4.8 0.1 0.9 NH1 B:ARG360 4.9 0.8 1.0 CB B:ILE285 5.0 0.5 1.0 N B:CMH371 5.0 0.2 1.0 CE2 B:PHE289 5.0 0.2 1.0

Mercury binding site 9 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg264 b:0.8 occ:0.90 HG C:CMH264 0.0 0.8 0.9 CM C:CMH264 2.1 0.3 0.9 SG C:CMH264 2.3 0.2 1.0 N C:CMH264 2.9 68.1 1.0 CE1 C:TYR261 3.0 0.5 1.0 O C:TYR261 3.1 94.1 1.0 CB C:CMH264 3.2 62.0 1.0 CA C:CMH264 3.3 61.8 1.0 CD C:PRO222 3.3 92.6 1.0 CD1 C:TYR261 3.3 0.9 1.0 CZ C:TYR261 3.3 0.6 1.0 C C:GLY263 3.4 95.1 1.0 CA C:GLY263 3.7 0.2 1.0 N C:GLY263 3.8 69.6 1.0 CG C:TYR261 3.8 0.2 1.0 CE2 C:TYR261 3.8 0.7 1.0 CG C:PRO222 3.8 0.9 1.0 OH C:TYR261 3.9 0.7 1.0 C C:TYR261 4.0 0.9 1.0 CD2 C:TYR261 4.1 0.7 1.0 O C:GLY263 4.3 1.0 1.0 N C:TYR261 4.5 0.5 1.0 O C:LEU221 4.6 85.7 1.0 N C:PRO222 4.6 92.2 1.0 C C:ARG262 4.6 0.5 1.0 CA C:TYR261 4.6 0.6 1.0 CB C:TYR261 4.8 92.5 1.0 C C:CMH264 4.8 0.3 1.0 N C:ARG262 4.9 0.7 1.0

Mercury binding site 10 out of 16 in the Crystal Structure of Translation Elongation Factor Selb From Methanococcus Maripaludis, Apo Form


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, Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Hg338 b:0.2 occ:0.70 HG C:CMH338 0.0 0.2 0.7 CM C:CMH338 2.1 73.0 0.7 SG C:CMH338 2.4 0.1 1.0 O C:GLU337 3.0 0.8 1.0 CB C:CMH338 3.3 79.8 1.0 CA C:CMH338 3.4 0.2 1.0 C C:GLU337 3.5 96.4 1.0 N C:CMH338 3.7 93.6 1.0 CD1 C:LEU329 4.3 0.1 1.0 N C:GLU337 4.4 93.1 1.0 CB C:LYS316 4.4 92.2 1.0 CA C:GLU337 4.6 74.3 1.0 C C:CMH338 4.8 95.0 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